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Space Group R3 (space + group_r3)
Selected AbstractsRedetermination of bis[,3 -1,3,5-triamino-1,3,5-trideoxy- cis -inositolato(3,)]tribismuth(III) trichloride hexahydrateACTA CRYSTALLOGRAPHICA SECTION C, Issue 1 2009Kaspar Hegetschweiler The crystal structure of the title compound, [Bi3(C6H12N3O3)2]Cl3·6H2O, which was described in the space group R3 [Hegetschweiler, Ghisletta & Gramlich (1993). Inorg. Chem.32, 2699,2704], has been redetermined in the revised space group R32 as suggested by Marsh [Acta Cryst. (2002), B58, 893,899]. Accordingly, the significant difference in the Bi,N bond distances of 2.43,(2) and 2.71,(1),Å, as noted in the previous study, proved to be an artifact. As a consequence, the [Bi3(H,3taci)2]Cl6/3 entity (taci is 1,3,5-triamino-1,3,5-trideoxy- cis -inositol) adopts D3 symmetry and the three Bi atoms lie on C2 axes with equal Bi,N bond distances of 2.636,(3),Å. [source] Structure of human TSG101 UEV domainACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2006Pedro L. Mateo The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6,Å, , = , = 90, , = 120°. Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2,Å resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition. [source] Crystallization and preliminary crystallographic studies of MOMP (major outer membrane protein) from Campylobacter jejuniACTA CRYSTALLOGRAPHICA SECTION D, Issue 12-2 2004Jean Michel Bolla Campylobacter jejuni is the leading bacterial cause of human enteritis linked to ingestion of contaminated food or water. MOMP, the major outer membrane protein from these Gram-negative bacteria, belongs to the porin family. In order to determine the three-dimensional structure of this protein and to elucidate the underlying molecular mechanisms, the MOMP from C. jejuni strain 85H has been purified and crystallized by vapour diffusion. Two crystal forms were characterized for this membrane protein. X-ray diffraction data were collected to a resolution of 3.1,Å using a synchrotron-radiation source from the orthorhombic crystal form, which belonged to space group P21212 with unit-cell parameters a = 170.1, b = 101.9, c = 104.9,Å. With a trimer in the asymmetric unit, the solvent content is 64% (VM = 3.4,Å,Da,1). The other form exhibits trigonal symmetry (space group R3) with hexagonal unit-cell parameters a = b = 94.2, c = 161.2,Å, but diffracts X-rays poorly to about 4,Å with significant anisotropy. [source] Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshiiACTA CRYSTALLOGRAPHICA SECTION D, Issue 10 2004Ryuya Fukunaga The leucyl-tRNA synthetase (LeuRS) from the archaeon Pyrococcus horikoshii was overexpressed in a C-terminally truncated form in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43,Å, , = , = 90, , = 120°. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2,Å3,Da,1 and a solvent content of 60.7%. A data set diffracting to 2.2,Å resolution was collected from a single crystal at 100,K. Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the SAD phasing method. [source] Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damageACTA CRYSTALLOGRAPHICA SECTION D, Issue 6 2004Viswanath Bandaru DNA glycosylases repair oxidative DNA damage caused by free radicals. Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types of pyrimidine-base damage. An active C-terminal deletion construct of NEIL1 was overexpressed in E. coli and crystallized. The unliganded NEIL1 crystallizes in space group R3, with unit-cell parameters a = b = 132.2, c = 51.1,Å. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4,Å, respectively. [source] Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritimaACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2002Michael A. McDonough Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit-cell parameters were obtained under two different conditions. The first, 0.3,M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2,mm in one week that diffracted to a resolution of 1.87,Å and had unit-cell parameters a = b = 80.6, c = 148.8,Å. The second, 0.1,M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1,Å and had unit-cell parameters a = b = 80.0, c = 150.1,Å. [source] Cloning, overexpression, purification, crystallization and preliminary X-ray analysis of CheY3, a response regulator that directly interacts with the flagellar `switch complex' in Vibrio choleraeACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2010Susmita Khamrui Vibrio cholerae is the aetiological agent of the severe diarrhoeal disease cholera. This highly motile organism uses the processes of motility and chemotaxis to travel and colonize the intestinal epithelium. Chemotaxis in V. cholerae is far more complex than that in Escherichia coli or Salmonella typhimurium, with multiple paralogues of various chemotaxis genes. In contrast to the single copy of the chemotaxis response-regulator protein CheY in E. coli, V. cholerae contains four CheYs (CheY1,CheY4), of which CheY3 is primarily responsible for interacting with the flagellar motor protein FliM, which is one of the major constituents of the `switch complex' in the flagellar motor. This interaction is the key step that controls flagellar rotation in response to environmental stimuli. CheY3 has been cloned, overexpressed and purified by Ni,NTA affinity chromatography followed by gel filtration. Crystals of CheY3 were grown in space group R3, with a calculated Matthews coefficient of 2.33,Å3,Da,1 (47% solvent content) assuming the presence of one molecule per asymmetric unit. [source] Improvement of the quality of lumazine synthase crystals by protein engineeringACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2008Lidia Rodríguez-Fernández Icosahedral macromolecules have a wide spectrum of potential nanotechnological applications, the success of which relies on the level of accuracy at which the molecular structure is known. Lumazine synthase from Bacillus subtilis forms a 150,Å icosahedral capsid consisting of 60 subunits and crystallizes in space group P6322 or C2. However, the quality of these crystals is poor and structural information is only available at 2.4,Å resolution. As classical strategies for growing better diffracting crystals have so far failed, protein engineering has been employed in order to improve the overexpression and purification of the molecule as well as to obtain new crystal forms. Two cysteines were replaced to bypass misfolding problems and a charged surface residue was replaced to force different molecular packings. The mutant protein crystallizes in space group R3, with unit-cell parameters a = b = 313.02, c = 365.77,Å, , = , = 90.0, , = 120°, and diffracts to 1.6,Å resolution. [source] Cloning, expression, purification, crystallization and preliminary crystallographic study of the protein module (BIV2-Helix) in the fusion core of bovine immunodeficiency-like virus (BIV) gp40ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2005Xiaodong Zhao The fusion core of bovine immunodeficiency virus (BIV) gp40 is proposed to be involved in membrane fusion. However, no crystal structures are yet available. A predicted protein module BIV2-Helix of BIVgp40 has been expressed in Escherichia coli and purified by chromatography. Recombinant BIV2-Helix was crystallized using the hanging-drop vapour-diffusion technique at 291,K. The crystals were grown in MPD and belonged to the primitive rhombohedral space group R3, with unit-cell parameters a = 39.17, b = 39.17, c = 295.05,Å and two molecules per asymmetric unit. X-ray diffraction data were collected to 1.76,Å in the home laboratory from a single crystal. [source] | ||||||||||