Crystallographic Analysis (crystallographic + analysis)

Distribution by Scientific Domains
Distribution within Chemistry

Kinds of Crystallographic Analysis

  • neutron crystallographic analysis
  • preliminary crystallographic analysis
  • preliminary x-ray crystallographic analysis
  • x-ray crystallographic analysis

  • Selected Abstracts

    Synthesis, X-Ray Crystallographic Analysis and Antitumor Activity of 3,6-Bis(substitutedphenyl)-1,4-bis (substitutedphenylsulfonyl)-1,4-dihydro-1,2,4,5-tetrazine.

    CHEMINFORM, Issue 40 2006
    Wei-Xiao Hu
    Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF. [source]

    Anilinopyrazole as Selective CDK2 Inhibitors: Design, Synthesis, Biological Evaluation, and X-Ray Crystallographic Analysis.

    CHEMINFORM, Issue 50 2003
    Jun Tang
    Abstract For Abstract see ChemInform Abstract in Full Text. [source]

    [(Pyridylcarbonyl)pyridyl]triazolopyridines, Useful Ligands for the Construction of Polynuclear Coordination Compounds , Synthesis, Crystal Structure and Magnetic Properties of a Novel Tetranuclear Copper(II) Cubane,

    Belén Abarca
    Abstract A new tetranuclear cubane Cu4O4 complex has been synthesised from assembly of CuII ions and the polydentate ligand (pyridin-2-yl){6-([1,2,3]triazolo[1,5- a]pyridin-3-yl)pyridin-2-yl}methanone. Crystallographic analysis indicates that the Cu4O4 unit has an S4 symmetry. The magnetic properties have been analysed using the H = ,2,i,jJijSiSj spin Hamiltonian. Two distinct coupling constants, 2J1,3 = ,37.4 cm,1 and 2J1,2 = ,2.6 cm,1, obtained from the fitting of the experimental data have been rationalised on the basis of a density functional study of magnetostructural correlations in cubane complexes containing the Cu4O4 core. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007) [source]

    The oxidation process of Antarctic fish hemoglobins

    FEBS JOURNAL, Issue 9 2004
    Luigi Vitagliano
    Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation process, promoted by air or ferricyanide, of five hemoglobins extracted from Antarctic fishes (Notothenioidei). Spectroscopic analysis revealed that these hemoglobins share a common oxidation pathway, which shows striking differences from the oxidation processes of hemoglobins from other vertebrates. Indeed, simple exposure of these hemoglobins to air leads to the formation of a significant amount of the low-spin hexacoordinated form, denoted hemichrome. This hemichrome form, which is detected under a variety of experimental conditions, can be reversibly transformed to either carbomonoxy or deoxygenated forms with reducing agents. Interestingly, the spectra of the fully oxidized species, obtained by treating the protein with ferricyanide, show the simultaneous presence of peaks corresponding to different hexacoordinated states, the aquomet and the hemichrome. In order to assign the heme region state of the , and , chains, the air-oxidized and ferricyanide-oxidized forms of Trematomus bernacchii hemoglobin were crystallized. Crystallographic analysis revealed that these forms correspond to an ,(aquomet)-,(bishistidyl-hemichrome) state. This demonstrates that the , and , chains of Antarctic fish hemoglobins follow very different oxidation pathways. As found for Trematomus newnesi hemoglobin in a partial hemichrome state [Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A. & Mazzarella, L. (2002) Proc. Natl Acad. Sci. USA99, 9801,9806], the quaternary structures of these ,(aquomet)-,(bishistidyl-hemichrome) forms are intermediate between the physiological R and T hemoglobin states. Together, these structures provide information on the general features of this intermediate state. [source]

    Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as established by chemical rescue experiments

    FEBS JOURNAL, Issue 22 2001
    Sébastien Dementin
    Enzymes MurD, MurE, MurF, folylpolyglutamate synthetase and cyanophycin synthetase, which belong to the Mur synthetase superfamily, possess an invariant lysine residue (K198 in the Escherichia coli MurD numbering). Crystallographic analysis of MurD and MurE has recently shown that this residue is present as a carbamate derivative, a modification presumably essential for Mg2+ binding and acyl phosphate formation. In the present work, the importance of the carbamoylated residue was investigated in MurD, MurE and MurF by site-directed mutagenesis and chemical rescue experiments. Mutant proteins MurD K198A/F, MurE K224A and MurF K202A, which displayed low enzymatic activity, were rescued by incubation with short-chain carboxylic acids, but not amines. The best rescuing agent was acetate for MurD K198A, formate for K198F, and propionate for MurE K224A and MurF K202A. In the last of these, wild-type levels of activity were recovered. A complementarity between the volume of the residue replacing lysine and the length of the carbon chain of the acid was noted. These observations support a functional role for the carbamate in the three Mur synthetases. Experiments aimed at recovering an active enzyme by introducing an acidic residue in place of the invariant lysine residue were also undertaken. Mutant protein MurD K198E was weakly active and was rescued by formate, indicating the necessity of correct positioning of the acidic function with respect to the peptide backbone. Attempts at covalent rescue of mutant protein MurD K198C failed because of its lack of reactivity towards haloacids. [source]

    Kinetic and crystallographic analysis of complexes formed between elastase and peptides from ,-casein

    FEBS JOURNAL, Issue 10 2001
    Penny A. Wright
    Human ,-casomorphin-7 (NH2 -Tyr-Pro-Phe-Val-Glu-Pro-Ile-CO2H) is a naturally occurring peptide inhibitor of elastase that has been shown to form an acyl-enzyme complex stable enough for X-ray crystallographic analysis at pH 5. To investigate the importance of the N-terminal residues of the ,-casomorphin-7 peptide for the inhibition of elastase, kinetic and crystallographic analyses were undertaken to identify the minimum number of residues required for effective formation of a stable complex between truncated ,-casomorphin-7 peptides and porcine pancreatic elastase (PPE). The results clearly demonstrate that significant inhibition of PPE can be effected by simple tri-, tetra-and pentapeptides terminating in a carboxylic acid. These results also suggest that in vivo regulation of protease activity could be mediated via short peptides as well as by proteins. Crystallographic analysis of the complex formed between N -acetyl-Val-Glu-Pro-Ile-CO2H and PPE at pH 5 (to 1.67 Å resolution) revealed an active site water molecule in an analogous position to that observed in the PPE/,-casomorphin-7 structure supportive of its assignment as the ,hydrolytic water' in the deacylation step of serine protease catalysis. [source]

    Crystallographic evidence of Gly- d,l -Met oxidation to its sulfoxide in the presence of gold(III): solid solution of the racemic mixture of two diastereoisomers

    Urszula Rychlewska
    Crystallographic analysis of a solid solution of two diastereoisomers, i.e. ({(1S,R)-1-carboxy-3-[(R,S)-methylsulfinyl]propyl}aminocarbonyl)methanaminium tetrachloridoaurate(III) and ({(1S,R)-1-carboxy-3-[(S,R)-methylsulfinyl]propyl}aminocarbonyl)methanaminium tetrachloridoaurate(III), (C7H15N2O4S)[AuCl4], has shown that in the presence of gold(III), the methionine part of the Gly- d,l -Met dipeptide is oxidized to sulfoxide, and no coordination to the AuIII cation through the S atom of the sulfoxide is observed. In view of our observation, literature reports that methionine acts as an N,S -bidentate donor ligand forming stable gold(III) complexes require verification. Moreover, it has been demonstrated that crystallization of the oxidation product leads to a substantial 77:23 excess of both S -methionine/R -sulfoxide and R -methionine/S -sulfoxide over S -methionine/S -sulfoxide and R -methionine/R -sulfoxide. The presence of two different diastereoisomers at the same crystallographic site is a source of static disorder at this site. [source]

    Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus

    Vaheh Oganesyan
    The crystal structure of a hypothetical protein AQ_1354 (gi 2983779) from the hyperthermophilic bacteria Aquifex aeolicus has been determined using X-ray crystallography. As found in many structural genomics studies, this protein is not associated with any known function based on its amino-acid sequence. PSI-BLAST analysis against a non-redundant sequence database gave 68 similar sequences referred to as `conserved hypothetical proteins' from the uncharacterized protein family UPF0054 (accession No. PF02310). Crystallographic analysis revealed that the overall fold of this protein consists of one central ,-helix surrounded by a four-stranded ,-sheet and four other ,-helices. Structure-based homology analysis with DALI revealed that the structure has a moderate to good resemblance to metal-dependent proteinases such as collagenases and gelatinases, thus suggesting its possible molecular function. However, experimental tests for collagen­ase and gelatinase-type function show no detectable activity under standard assay conditions. Therefore, we suggest either that the members of the UPF0054 family have a similar fold but different biochemical functions to those of collagenases and gelatinases or that they have a similar function but perform it under different conditions. [source]

    Crystallization and preliminary X-ray analysis of the complex of human ,-thrombin with a modified thrombin-binding aptamer

    Irene Russo Krauss
    The thrombin-binding aptamer (TBA) is a consensus DNA 15-mer that binds specifically to human ,-thrombin at nanomolar concentrations and inhibits its procoagulant functions. Recently, a modified TBA (mTBA) containing a 5,,5, inversion-of-polarity site has been shown to be more stable and to possess a higher thrombin affinity than its unmodified counterpart. The structure of the thrombin,TBA complex has previously been determined at low resolution, but did not provide a detailed picture of the aptamer conformation or of the protein,DNA assembly, while that of the complex with mTBA is unknown. Crystallographic analysis of the thrombin,mTBA complex has been attempted. The crystals diffracted to 2.15,Å resolution and belonged to space group I222. [source]

    Synthesis and Reactivity of the Monomeric Late-Transition-Metal Parent Amido Complex [Ir(Cp*)(PMe3)(Ph)(NH2)]

    Daniela Rais Dr.
    Abstract The late-transition-metal parent amido compound [Ir(Cp*)(PMe3)(Ph)(NH2)] (2) has been synthesized by deprotonation of the corresponding ammine complex [Ir(Cp*)(PMe3)(Ph)(NH3)][OTf] (6) with KN(SiMe3)2. An X-ray structure determination has ascertained its monomeric nature. Proton-transfer studies indicate that 2 can successfully deprotonate p -nitrophenylacetonitrile, aniline, and phenol. Crystallographic analysis has revealed that the ion pair [Ir(Cp*)(PMe3)(Ph)(NH3)][OPh] (8) exists as a hydrogen-bonded dimer in the solid state. Reactions of 2 with isocyanates and carbodiimides lead to overall insertion of the heterocumulenes into the NH bond of the Ir-bonded amido group, demonstrating the ability of 2 to act as an efficient nucleophile. Intriguing reactivity is observed when amide 2 reacts with CO or 2,6-dimethylphenyl isocyanide. ,4 -Tetramethylfulvene complexes [Ir(,4 -C5Me4CH2)(PMe3)(Ph)(L)] (L=CO (15), CNC6H3 -2,6-(CH3)2 (16)) are formed in solution through displacement of the amido group by the incoming ligand followed by deprotonation of a methyl group on the Cp* ring and liberation of ammonia. Conclusive evidence for the presence of the Ir-bonded ,4 -tetramethylfulvene moiety in the solid state has been provided by an X-ray diffraction study of complex 16. [source]

    Structure-Dependent Electrochemical Behavior of Thienylplatinum(II) Complexes of N,N-Heterocycles

    Feng Zhao
    Abstract trans -[Pt(MeCN)(PPh3)2(2-thienyl)]BF4 (1) serves as a convenient precursor to bifunctional mononuclear trans -[Pt(PPh3)2(,1 - N - N)(2-thienyl)]BF4 [N - N = pyrazine (2); 2-chloropyrazine, (3)] and dinuclear trans,trans -[Pt2(PPh3)4(,- N - N)(2-thienyl)2](BF4)2 [(N - N = 4,4, -bipyridine (4); 4,4, -vinylenedipyridine (5)] complexes. The nuclear selectivity is conveniently controlled by the choice of the heterocyclic ligands or spacers. Both structural types 3 and 5 were confirmed by single-crystal X-ray crystallographic analyses. Their solution identities were established by positive-ion Electrospray Mass Spectrometry (ESMS). The electroactivities of these complexes were studied by cyclic voltammetry (CV). Continuous CV scans of 4 and 5 revealed variations in the redox waves with the number of scans. While the initial oxidative scan exhibited only a broad, irreversible wave, further cycling showed the growth of two additional redox couples up to about the tenth cycle. The peak currents of these redox couples began to decay with prolonged potential cycling beyond the tenth cycle. These findings are consistent with the formation of electroactive oligomers/polymers, and this conclusion is supported by visible thin film formation on the electrodes. In contrast, the mononuclear complexes (2 and 3) do not show such behavior. The films formed were further studied by repetitive potential cycling and XPS. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004) [source]

    Synthesis and Absolute Configuration of (+)-Pseudodeflectusin: Structural Revision of Aspergione B

    Fumiyo Saito
    Abstract We report herein the total synthesis and determination of the absolute configuration of (+)-pseudodeflectusin. The total synthesis of (+)-pseudodeflectusin starting from o -anisic aid was achieved in 11 total steps with an overall yield of 2.0,%. The 1H- and 13C NMR spectroscopic data of our synthetic pseudodeflectusin was identical to that of the natural compound. The absolute configuration of (+)-pseudodeflectusin was determined by chiral HPLC and X-ray crystallographic analyses. We also synthesized the proposed structure of aspergione B, whose 1H- and 13C NMR spectroscopic data is identical to that of pseudodeflectusin. The 1H- and 13C NMR spectra of our synthetic aspergione B were different from those of the natural compound reported by Proksch et al. Our results confirm that aspergione B and pseudodeflectusin are, in fact, the same compound.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006) [source]

    Destabilization of psychrotrophic RNase HI in a localized fashion as revealed by mutational and X-ray crystallographic analyses

    FEBS JOURNAL, Issue 2 2009
    Muhammad S. Rohman
    The Arg97 , Gly and Asp136 , His mutations stabilized So-RNase HI from the psychrotrophic bacterium Shewanella oneidensis MR-1 by 5.4 and 9.7 °C, respectively, in Tm, and 3.5 and 6.1 kJ·mol,1, respectively, in ,G(H2O). These mutations also stabilized the So-RNase HI derivative (4×-RNase HI) with quadruple thermostabilizing mutations in an additive manner. As a result, the resultant sextuple mutant protein (6×-RNase HI) was more stable than the wild-type protein by 28.8 °C in Tm and 27.0 kJ·mol,1 in ,G(H2O). To analyse the effects of the mutations on the protein structure, the crystal structure of the 6×-RNase HI protein was determined at 2.5 Å resolution. The main chain fold and interactions of the side-chains of the 6×-RNase HI protein were basically identical to those of the wild-type protein, except for the mutation sites. These results indicate that all six mutations independently affect the protein structure, and are consistent with the fact that the thermostabilizing effects of the mutations are roughly additive. The introduction of favourable interactions and the elimination of unfavourable interactions by the mutations contribute to the stabilization of the 6×-RNase HI protein. We propose that So-RNase HI is destabilized when compared with its mesophilic and thermophilic counterparts in a localized fashion by increasing the number of amino acid residues unfavourable for protein stability. [source]

    Kinetic and crystallographic analysis of complexes formed between elastase and peptides from ,-casein

    FEBS JOURNAL, Issue 10 2001
    Penny A. Wright
    Human ,-casomorphin-7 (NH2 -Tyr-Pro-Phe-Val-Glu-Pro-Ile-CO2H) is a naturally occurring peptide inhibitor of elastase that has been shown to form an acyl-enzyme complex stable enough for X-ray crystallographic analysis at pH 5. To investigate the importance of the N-terminal residues of the ,-casomorphin-7 peptide for the inhibition of elastase, kinetic and crystallographic analyses were undertaken to identify the minimum number of residues required for effective formation of a stable complex between truncated ,-casomorphin-7 peptides and porcine pancreatic elastase (PPE). The results clearly demonstrate that significant inhibition of PPE can be effected by simple tri-, tetra-and pentapeptides terminating in a carboxylic acid. These results also suggest that in vivo regulation of protease activity could be mediated via short peptides as well as by proteins. Crystallographic analysis of the complex formed between N -acetyl-Val-Glu-Pro-Ile-CO2H and PPE at pH 5 (to 1.67 Å resolution) revealed an active site water molecule in an analogous position to that observed in the PPE/,-casomorphin-7 structure supportive of its assignment as the ,hydrolytic water' in the deacylation step of serine protease catalysis. [source]

    Concerning the Structure of [18]Annulene

    Otto Ermer
    A recent computational study of Schleyer and co-workers [1] is reviewed, which led these authors to the firm conclusion that [18]annulene has a localized structure with alternating single and double C,C bonds, contrary to earlier crystallographic analyses of X-ray-diffraction data favoring a delocalized non-alternating form. It is pointed out i) that deceptive orientational disorder phenomena in the crystal might be subject to experimental resolution in this case, and ii) that, in contrast to gas and solution phases, [18]annulene might possibly assume the non-alternating structure in the crystalline solid state. [source]

    Syntheses and crystal structures of triorganotin (IV) derivatives with 2,2,-bipyridine-4,4,-dicarboxylic acid

    Ru-Fen Zhang
    Four organotin complexes with 2,2,-bipyridine-4,4,-dicarboxylic acid, H2dcbp: (Ph3n)2(dcbp) 1, [(PhCH2)3n]2(dcbp) , 2CH3OH 2, [(Me3Sn)2(dcbp)]n3, [(Bu3Sn)2(dcbp)]n4 have been synthesized. The complexes 1,4 were characterized by elemental, IR, 1H, 13C, 119n NMR, and X-ray crystallographic analyses. Crystal structures show that complex 1 is a monomer with one ligand coordinated to two triorganotin moieties, and a 1D infinite polymeric chain generates via intermolecular CH,,,N hydrogen bond; complex 2 is also a monomer and forms a 2D network by intermolecular O,H,,,O weak interaction; both of complexes 3 and 4 form 2D network structures where 2,2,-bipyridine-4,4,-dicarboxylate acts as a tetradentate ligand coordinated to trimethyltin and tri-n-butyltin ions, respectively. © 2009 Wiley Periodicals, Inc. Heteroatom Chem 20:19,28, 2009; Published online in Wiley InterScience ( DOI 10.1002/hc.20506 [source]

    Structures and properties of two diastereomeric cyclic sulfites derived from cis -3,4-di- tert -butylthiolane-3,4-diol and thionyl chloride

    Sanae Tanaka
    cis-3,4-Di-tert-butylthiolane-3,4-diol (1) was treated with an equimolar amount of thionyl chloride in the presence of triethylamine or pyridine in several solvents of different polarity to furnish two diastereomeric sulfites 2a and 2b generally in excellent combined yields. Although 2a was consistently formed as the major diastereomer when pyridine was used as the base, 2a and 2b were formed in approximately equal amounts when triethylamine was used as the base in polar solvents. X-ray crystallographic analyses revealed that the SO group of 2a is anti to the thiolane ring and that of 2b syn to the thiolane ring. Density functional theory calculations (B3LYP/6-31G* level) revealed that 2a is less stable than 2b by 1.28 kcal mol,1, although 2a was formed generally as the predominant diastereomer. Spectroscopic data of 2a and 2b are discussed with emphasis on comparison with those obtained by calculations. Treatment of 2a and 2b with m-chloroperbenzoic acid resulted in the oxidation of the divalent sulfur atom of the thiolane ring and not the sulfite sulfur atom. The above oxidations took place exclusively at the syn-side with respect to the tert-butyl groups.© 2003 Wiley Periodicals, Inc. Heteroatom Chem 14:587,595, 2003; Published online in Wiley InterScience ( DOI 10.1002/hc.10192 [source]

    20-Di­cyano­methyl­ene-5,8,11,14-tetraoxa-2,17-di­thia­bi­cyclo­[16.4.1]­tricosa-1(23),18,21-triene and its mercury(II) dichloride complex

    Kanji Kubo
    The structures of the title compound, C20H24N2O4S2, and its mercury(II) dichloride complex, dichloro{20-di­cyano­methyl­ene-5,8,11,14-tetraoxa-2,17-di­thia­bi­cyclo­[16.4.1]­tricosa-1(23),18,­21-tri­ene-,4O,,S17}mercury(II), [HgCl2(C20­H24­N2­O4­S2)], have been determined by X-ray crystallographic analyses. The mercury(II) dichloride complex has two independent mol­ecules of [HgCl2(C20H24N2O4S2)] in the lattice. The mercury(II) ion has pentagonal bipyramidal coordination which involves one S atom, four O atoms and two Cl, ions. [source]

    Purification, crystallization and preliminary X-ray analysis of Triatoma virus (TrV) from Triatoma infestans

    Gabriela S. Rozas-Dennis
    Triatoma virus (TrV) is a viral pathogen of the blood-sucking reduviid bug Triatoma infestans, the most important vector of American human trypanosomiasis (Chagas' disease). TrV has been putatively classified as a member of the Cripavirus genus (type cricket paralysis virus) in the Dicistroviridae family. This work describes the purification of TrV particles from infected T. infestans and their crystallization and preliminary crystallographic analyses. Two different crystal forms, rhombohedral and orthorhombic, were obtained at room temperature by the hanging-drop vapour-diffusion technique using polyethylene glycol and polyethylene glycol monomethylether as precipitants. The rhombohedral crystals have unit-cell parameters a = b = 306.6, c = 788.4,Å (hexagonal setting), diffract to 3.2,Å resolution and contain one-third of the viral particle per asymmetric unit. The orthorhombic crystals have cell parameters a = 336, b = 351, c = 332,Å, diffract to about 2.5,Å resolution, and contain one-half of a virus particle in the asymmetric unit. A complete diffraction data set has been collected to 3.2,Å resolution, using synchrotron radiation, from a single rhombohedral crystal under cryogenic conditions. [source]

    Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C ,-lactamases with extended substrate spectrum

    Sun-Joo Lee
    Plasmid-encoded class C ,-lactamases, including CMY-1 and CMY-­10, hydrolyze the lactam bonds of ,-lactam antibiotics, inducing therapeutic failure and a lack of eradication of clinical isolates by third-generation cephalosporins or cephamycins. Therefore, the enzymes are potential targets for developing agents against pathogens isolated from patients suffering from wound infection, urinary tract infection or pneumonia. CMY-1 and CMY-10 were purified and crystallized at 298,K. X-ray diffraction data from CMY-1 and CMY-­10 crystals have been collected to 2.5 and 1.5,Å resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P21. [source]

    Crystallization and preliminary X-ray analysis of a thermoalkalophilic lipase from Bacillus stearothermophilus L1

    Seong-Tae Jeong
    A thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) was crystallized in two different crystal forms using a low concentration of the enzyme and a calcium-exchange process. The first, needle-like, crystal form, which diffracts to about 3.5,Å, belongs to the orthorhombic space group P212121, with unit-cell parameters a = 67.84, b = 72.96, c = 104.41,Å. The second, monoclinic, crystal form, which behaves better than the first form for crystallographic analyses, belongs to the monoclinic space group C2 and has unit-cell parameters a = 119.62, b = 85.05, c = 98.36,Å, , = 99.73°. From the monoclinic crystals, a native data set and a samarium-derivative data set were collected to 2.0 and 2.3,Å resolution, respectively. The difference Patterson map between the two data sets shows strong heavy-atom peaks, indicating that the crystals are suitable for a high-resolution structure determination. [source]

    Crystallization and preliminary X-ray diffraction analysis of various enzyme,substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus

    Angelo Merli
    The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt -IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg2+ or Mn2+ and with the help of NAD+. In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt -IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported. [source]

    Crystallization and preliminary X-ray diffraction analysis of the fructofuranosidase from Schwanniomyces occidentalis

    Aitana Polo
    Schwanniomyces occidentalis invertase is an extracellular enzyme that releases ,-fructose from the nonreducing termini of various ,- d -fructofuranoside substrates. Its ability to produce 6-kestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The enzyme has been expressed in Saccharomyces cerevisiae. Recombinant and wild-type forms, which showed different glycosylation patterns, were crystallized by vapour-diffusion methods. Although crystallization trials were conducted on both forms of the protein, crystals suitable for X-ray crystallographic analyses were only obtained from the wild-type enzyme. The crystals belonged to space group P212121, with unit-cell parameters a = 105.78, b = 119.49, c = 137.68,Å. A diffraction data set was collected using a synchrotron source. Self-rotation function and sedimentation-velocity experiments suggested that the enzyme was dimeric with twofold symmetry. [source]

    Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 9

    Matthew Mitchell
    Adeno-associated virus (AAV) serotype 9, which is under development for gene-delivery applications, shows significantly enhanced capsid-associated transduction efficiency in muscle compared with other AAV serotypes. With the aim of characterizing the structural determinants of this property, the purification, crystallization and preliminary X-ray crystallographic analyses of the AAV9 viral capsid are reported. The crystals diffracted X-rays to 2.8,Å resolution using synchrotron radiation and belonged to the trigonal space group P32, with unit-cell parameters a = b = 251.0, c = 640.0,Å. There are three complete viral capsids in the crystal unit cell. The orientation and position of the asymmetric unit capsid have been determined by molecular-replacement methods and structure determination is in progress. [source]

    Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus

    Alessia Ruggiero
    The thioredoxin system of the archaeon Sulfolobus solfataricus involves a number of different proteins: two thioredoxin reductases (SsTrxRB2 and SsTrxRB3), two distinct thioredoxins (SsTrxA1 and SsTrxA2) and a disulfide oxidoreductase (SsPDO). Here, the crystallization and preliminary crystallographic analyses of SsTrxA1 and SsTrxA2, two dimeric proteins endowed with extraordinary thermal stability, are reported. In addition to the functional thioredoxin domain, both SsTrxA1 and SsTrxA2 present an extra N-terminal fragment of approximately 30 residues. Although crystallization trials have been conducted on both forms of the proteins, crystals that were suitable for X-ray crystallographic analyses have only been obtained for their truncated variants. The crystals of SsTrxA2 belonged to space group P2, with unit-cell parameters a = 28.27, b = 27.88, c = 62.06,Å, , = 92.34°, and diffracted to 1.83,Å resolution, whereas the crystals of SsTrxA1 belonged to space group P21, with unit-cell parameters a = 51.76, b = 75.09, c = 55.35,Å, , = 112.64°, and diffracted to 1.90,Å resolution. The structures of the two proteins have been solved by molecular replacement. [source]

    Two Regioisomers of Endohedral Pyrrolidinodimetallofullerenes M2@Ih -C80(CH2)2NTrt (M=La, Ce; Trt=trityl): Control of Metal Atom Positions by Addition Positions

    Michio Yamada Dr.
    Abstract The two regioisomers of endohedral pyrrolidinodimetallofullerenes M2@Ih -C80(CH2)2NTrt (M=La, Ce; Trt=trityl) were synthesized, isolated, and characterized. X-ray crystallographic analyses of [6,6]-La2@Ih -C80(CH2)2NTrt and [6,6]-Ce2@Ih -C80(CH2)2NTrt revealed that the encapsulated metal atoms are located at the slantwise positions on the mirror plane that parallels the pyrrolidine ring. Paramagnetic NMR analyses of [6,6]- and [5,6]-Ce2@Ih -C80(CH2)2NTrt were also carried out to clarify the metal positions. As for the [6,6]-adduct, the metal positions obtained by paramagnetic NMR analysis agree well with the X-ray structure. In contrast, paramagnetic NMR analysis of the [5,6]-adduct showed that the two Ce atoms are collinear with the pyrrolidine ring. We also compared the observed paramagnetic effects of the pyrrolidinodimetallofullerenes with those of other cerium-encapsulating fullerene derivatives such as bis-silylated Ce2@Ih -C80 and a carbene adduct of Ce2@Ih -C80. We found that the metal positions can be explained by the electrostatic potential maps of the corresponding [6,6]- and [5,6]-adducts of [Ih -C80(CH2)2NTrt]6,. These findings clearly show that metal positions inside fullerene cages can be controlled by means of the addition positions of the addends. In addition, the radical anions of the pyrrolidinodimetallofullerenes were prepared by bulk controlled-potential electrolysis and characterized by X-band EPR spectral study. [source]

    Structures and Solvatochromic Phosphorescence of Dicationic Terpyridyl,Platinum(II) Complexes with Foldable Oligo(ortho -phenyleneethynylene) Bridging Ligands

    Ming-Xin Zhu
    Abstract A series of binuclear organoplatinum(II) complexes, [(tBu3tpy)Pt(CC1,2-C6H4)nCCPt(tBu3tpy)][ClO4]2 (1,7, n=1, 2, 3, 4, 5, 6, 8; tBu3tpy=4,4,,4,,-tri- tert -butyl-2,2,:6,,2,,-terpyridine) with foldable oligo(ortho -phenyleneethynylene) linkers were prepared and characterized by spectroscopic methods and/or X-ray crystallographic analyses. In the crystal structures of 3,2.5,CH3OH, 5,CH3CN, and 6,4,CH3CN, each of the bridging ortho -phenyleneethynylene ligands has a partially folded conformation. In aerated water/acetonitrile mixtures with water percentages larger than 40,%, the emission of complexes 3,7 are red-shifted and enhanced when compared to those recorded in acetonitrile. The red-shift in emission energy and enhanced emission intensity can be attributed to the inter- and/or intramolecular interactions induced by the addition of water to solutions of the platinum(II) complexes in acetonitrile. Data from dynamic light scattering and transmission electron microscopy studies revealed that these binuclear platinum(II) complexes aggregated into nanosized particles in acetonitrile/water mixtures. Hydrophobic folding of the ortho -phenyleneethynylene linkers in acetonitrile/water mixtures is postulated. [source]

    Resolution, configurational assignment, and enantiopharmacology at glutamate receptors of 2-amino-3-(3-carboxy-5-methyl-4-isoxazolyl)propionic acid (ACPA) and demethyl-ACPA,

    CHIRALITY, Issue 9 2001
    Tommy N. Johansen
    Abstract We have previously described (RS)-2-amino-3-(3-carboxy-5-methyl-4-isoxazolyl)propionic acid (ACPA) as a potent agonist at the (RS)-2-amino-3-(3-hydroxy-5-methyl-4-isoxazolyl)propionic acid (AMPA) receptor subtype of (S)-glutamic acid (Glu) receptors. We now report the chromatographic resolution of ACPA and (RS)-2-amino-3-(3-carboxy-4-isoxazolyl)propionic acid (demethyl-ACPA) using a Sumichiral OA-5000 column. The configuration of the enantiomers of both compounds have been assigned based on X-ray crystallographic analyses, supported by circular dichroism spectra and elution orders on chiral HPLC columns. Furthermore, the enantiopharmacology of ACPA and demethyl-ACPA was investigated using radioligand binding and cortical wedge electrophysiological assay systems and cloned metabotropic Glu receptors. (S)-ACPA showed high affinity in AMPA binding (IC50 = 0.025 ,M), low affinity in kainic acid binding (IC50 = 3.6 ,M), and potent AMPA receptor agonist activity on cortical neurons (EC50 = 0.25 ,M), whereas (R)-ACPA was essentially inactive. Like (S)-ACPA, (S)-demethyl-ACPA displayed high AMPA receptor affinity (IC50 = 0.039 ,M), but was found to be a relatively weak AMPA receptor agonist (EC50 = 12 ,M). The stereoselectivity observed for demethyl-ACPA was high when based on AMPA receptor affinity (eudismic ratio = 250), but low when based on electrophysiological activity (eudismic ratio = 10). (R)-Demethyl-ACPA also possessed a weak NMDA receptor antagonist activity (IC50 = 220 ,M). Among the enantiomers tested, only (S)-demethyl-ACPA showed activity at metabotropic receptors, being a weak antagonist at the mGlu2 receptor subtype (KB = 148 ,M). Chirality 13:523,532, 2001. © 2001 Wiley-Liss, Inc. [source]

    An Efficient Route to Group 6 and 8 Metallaborane Compounds: Synthesis of arachno -[Cp*Fe(CO)B3H8] and closo -[(Cp*M)2B5H9] (M = Mo, W)

    K. Geetharani
    Abstract Reaction of [Cp*Fe(CO)2I] (Cp* = ,5 -C5Me5) with an excess amount of BH3·thf in toluene at 75 °C or with LiBH4 at ,78 °C leads to the isolation of hydrogen-rich ferraborane arachno -[Cp*Fe(CO)B3H8] in good yield. In a similar fashion, reaction of [Cp*M(CO)3Cl] (M = Mo and W) with an excess amount of BH3·thf at 80 °C or at ,78 °C with LiBH4 yielded metallaboranes [(Cp*M)2B5H9] (M = Mo, W). Isolated yields of closo -[(Cp*M)2B5H9], (M = Mo and W), both from LiBH4 and BH3·thf, are good. All compounds were characterized in solution by IR, 1H, 11B, and 13C NMR spectroscopy and mass spectrometry and the structural types were unequivocallyestablished by crystallographic analysis of arachno -[Cp*Fe(CO)B3H8].(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009) [source]

    The First Sandwich Complex with an Octa(thioether) Coordination Sphere: Bis(maleonitrile-tetrathia-12-crown-4)silver(I),

    Hans-Jürgen Holdt
    Abstract The new tetrathiacrown ethers maleonitrile-tetrathia-12-crown-4 (mn12S4) and maleonitrile-tetrathia-13-crown-4 (mn13S4) have been prepared and characterised by X-ray crystallographic analysis. These crown ethers form 2:1, 3:2 and 1:1 complexes with AgY (Y = BF4, PF6). The crystal structures of [Ag(mn12S4)2]BF4 (3a), [Ag(mn13S4)2]BF4 (4a) and [Ag2(mn13S4)3](PF6)2 (6b) have been determined. Compound 3a contains the centrosymmetric sandwich complex cation [Ag(mn12S4)2]+ where each mn12S4 ligand is coordinated to the Ag centre in an endo manner through all four S atoms. The 2:1 complex [Ag(mn12S4)2]+ is the first sandwich complex with a tetrathiacrown ether and the first complex with an octa(thioether) coordination sphere. The crystal structure of compound 4a also reveals a 2:1 complex. This complex, [Ag(mn13S4)2]+, exhibits a half-sandwich structure. One mn13S4 ligand coordinates to Ag+ by all four S donor atoms and the other 13S4 crown by only one S atom. Compound 6b contains a dinuclear Ag complex. The Ag complexes 3a,b,8a,b were also studied by electrospray ionisation mass spectrometry. Collision-induced dissociation (CID) was used to compare the relative stability of 2:1 complexes [AgL2]+ and 1:1 complexes [AgL]+ (L = mn12S4, mn13S4). The 13C NMR chemical shifts of 2:1 and 1:1 Ag complexes and their corresponding free ligands were also estimated and compared. The free energy of the barrier of ring inversion (,G,) for [Ag(mn12S4)2]+ was determined to be 64 kJ,mol,1. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006) [source]