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X-ray Structural Studies (x-ray + structural_studies)

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Chemistry	100%

Selected Abstracts

Solution NMR and X-Ray Structural Studies on Phthalocyaninatoiron Complexes

HELVETICA CHIMICA ACTA, Issue 8 2006
Ignacio Fernández
Abstract The addition of primary amines as solubilizing reagents for phthalocyaninatoiron complexes is shown to afford six-coordinate bis(amine)phthalocyaninato complexes, i.e., [Fe(amine)2(pc)] 2 (amine,=,decan-1-amine) and 3 (amine,=,benzylamine), with the two new N-donors occupying the trans -axial positions. The new complexes were characterized by extensive NMR measurements in THF solution. For complex 3 with the benzylamine ligand, the solid-state structure was determined by X-ray diffraction methods. Complex 2 is sufficiently labile in THF solution to exchange one amine ligand against CO (gas) affording an equilibrium mixture containing [Fe(amine)(CO)(pc)] 4. [source]

Reactivity and X-ray Structural Studies in Ligand Substitution of [Cp/(Ind)Ru(dppf)Cl] , Epimerisation in [Cp/(Ind)Ru(Josiphos)Cl] {Cp = ,5 -C5H5, Ind = ,5 -C7H9, dppf = 1,1,-Bis(diphenylphosphanyl)ferrocene, Josiphos = (R)-(,)-1-[(S)-2-(Diphenylphosphanyl)ferrocenyl]ethyldicyclohexylphosphane}

EUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 3 2007
Sin Yee Ng
Abstract Ligand substitution of [(Ind)Ru(PPh3)2Cl] (1) led to the isolation of [(Ind)Ru(PPh3){Ph2P(CH2)2C9H7}Cl] (2), [(Ind)Ru(dppf)Cl] (3) and [(Ind)Ru{(Ph2PCH2)3CMe}]PF6 ([4]PF6), and diastereoisomers [(R)- and (S)-(Ind)Ru(Josiphos)Cl] [(R)- 5 and (S)- 5], where (R)-(S)-Josiphos is the ferrocene-based chiral diphosphane ligand (R)-(,)-1-[(S)-2-(diphenylphosphanyl)ferrocenyl] ethyldicyclohexylphosphane. The Cp analogues of 5, viz. (R)- 6 and (S)- 6, were also obtained from [CpRu(PPh3)2Cl] (1a). Josiphos-dependent epimerisation was observed, with conversion of the (S) isomer to the (R) isomer in both cases. Chloride abstraction of 3 with NaPF6 in CH3CN and NaN3 in EtOH gave [(Ind)Ru(dppf)(CH3CN)]PF6 ([7]PF6) and [(Ind)Ru(dppf)(N3)] (8), respectively. The azido ligand in 8 underwent [3+2] dipolar cycloaddition with dimethyl acetylenedicarboxylate to give a N -bound bis(methoxycarbonyl)-1,2,3-triazolato complex, 9. X-ray crystal structures of the new complexes, except (R)- 5, (S)- 5 and (S)- 6, have been determined. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007) [source]

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. oryzae

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2009
Kim-Hung Huynh
Xanthomonas oryzae pv. oryzae (Xoo) causes the serious disease bacterial blight in rice. The pepA (Xoo0834) gene from Xoo is one of around 100 genes that have been selected for the design of antibacterial drugs. The pepA gene encodes leucine aminopeptidase (LAP), an exopeptidase that catalyzes the hydrolysis of leucine residues from the N-terminus of a protein or peptide. This enzyme was expressed in Escherichia coli, purified and crystallized, and preliminary X-ray structural studies have been carried out. The LAP crystal diffracted to 2.6,Å resolution and belonged to the cubic space group P213. The unit-cell volume of the crystal was compatible with the presence of two monomers in the asymmetric unit. [source]

Crystallization and preliminary X-ray structural studies of human prouroguanylin.

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2008
Corrigendum
A correction is made to the list of authors for Itoet al. [Acta Cryst. (2008). F64, 531,532]. [source]

Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein domain III

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2005
Zhiyong Lou
Domain III of the West Nile virus envelope protein, the putative receptor-binding domain, is a major virion-surface determinant for virulence. This protein was reported to be intrinsically unstable and has defied previous crystallization attempts. It has now been purified from inclusion bodies by protein refolding and was crystallized using the hanging-drop vapour-diffusion method at 291,K. The crystals belong to space group P2221, with unit-cell parameters a = 52.6, b = 59.7, c = 95.0,Å. A complete data set was collected to 2.8,Å at 100,K with Cu,K, X-rays from a rotating-anode generator. [source]