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Complete Native Data Set (complete + native_data_set)
Selected AbstractsCrystallization and preliminary crystallographic study of the functional form of the Bacillus thuringiensis mosquito-larvicidal Cry4Aa mutant toxinACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2004Panadda Boonserm The 65,kDa functional form of the mosquito-larvicidal Cry4Aa-R235Q mutant toxin has been crystallized. The crystals belong to space group C2221, with unit-cell parameters a = 91.2, b = 202.1, c = 98.7,Å, and contain one molecule per asymmetric unit. The crystals diffract to ,2.9,Å using synchrotron radiation and a complete native data set has been collected. The structure has been solved using a molecular-replacement method with the Cry4Ba toxin protein as a search model. [source] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of HP1352, a putative DNA methyltransferase in Helicobacter pyloriACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2003Katja Schirwitz The putative methyltransferase gene HP1352 from Helicobacter pylori strain 26695 was heterologously expressed in Escherichia coli. The 359-amino-acid gene product was purified and crystallized. The crystals belong to space group I212121 and show diffraction to at least 2.5,Å resolution. The unit-cell parameters are a = 69.6, b = 86.6, c = 140.0,Å. A greater than 90% complete native data set has been collected and structure determination using the molecular-replacement method is ongoing. [source] Crystallization and preliminary X-ray diffraction analysis of Thermus thermophilus prolyl-tRNA synthetaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2000Anna Yaremchuk Prolyl-tRNA synthetase from Thermus thermophilus (ProRSTT) was purified to homogeneity using a five-step purification procedure and was crystallized using ethylene glycol as a precipitant. Crystals of ProRSTT belong to the space group P21212, with unit-cell parameters a = 132, b = 191, c = 125,Å, have two homodimers per asymmetric unit and diffract to 2.4,Å resolution. A complete native data set to 2.43,Å resolution has been collected and a data set from ProRSTT in complex with proline has been collected to 2.9,Å resolution. [source] Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid proteinACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2010I-Jung Chen The N-terminal domain of nucleocapsid protein from human coronavirus OC43 (HCoV-OC43 N-NTD) mostly contains positively charged residues and has been identified as being responsible for RNA binding during ribonucleocapsid formation in the coronavirus. In this study, the crystallization and preliminary crystallographic analysis of HCoV-OC43 N-NTD (amino acids 58,195) with a molecular weight of 20,kDa are reported. HCoV-OC43 N-NTD was crystallized at 293,K using PEG 1500 as a precipitant and a 99.9% complete native data set was collected to 1.7,Å resolution at 100,K with an overall Rmerge of 5.0%. The crystals belonged to the hexagonal space group P65, with unit-cell parameters a = 81.57, c = 42.87,Å. Solvent-content calculations suggest that there is likely to be one subunit of N-NTD in the asymmetric unit. [source] Purification, crystallization and preliminary X-ray diffraction analysis of the lytic transglycosylase MltF from Escherichia coliACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2010Pramod K. Madoori The lytic transglycosylase MltF from Escherichia coli is an outer-membrane-bound periplasmic protein with two domains: a C-terminal catalytic domain with a lysozyme-like fold and an N-terminal domain of unknown function that is homologous to the periplasmic substrate-binding proteins of ABC transporters. In order to investigate its structure and function, a soluble form of full-length MltF (sMltF) containing both domains and a soluble fragment containing only the N-terminal domain (sMltF-NTD) were purified and crystallized. Crystals of sMltF belonged to space group P43212 or P41212, with unit-cell parameters a = b = 110.8, c = 163.5,Å and one or two molecules per asymmetric unit. A complete data set was collected to 3.5,Å resolution. Crystals of sMltF-NTD belonged to space group P3121, with unit-cell parameters a = b = 82.4, c = 75.2,Å and one molecule per asymmetric unit. For sMltF-NTD, a complete native data set was collected to 2.20,Å resolution. In addition, for phasing purposes, a three-wavelength MAD data set was collected to 2.5,Å resolution using a bromide-soaked sMltF-NTD crystal. Using phases derived from the Br-MAD data, it was possible to build a partial model of sMltF-NTD. [source] Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37RvACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2010Bernhard Sielaff Full-length GroEL1 from Mycobacterium tuberculosis H37Rv was cloned, overexpressed and purified. Crystals were obtained by the hanging-drop vapor-diffusion method and contained a 23,kDa GroEL1 fragment. A complete native data set was collected from a single frozen crystal that belonged to the orthorhombic space group P21212, with unit-cell parameters a = 75.47, b = 78.67, c = 34.89,Å, , = , = , = 90°, and diffracted to 2.2,Å resolution on a home X-ray source. [source] Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2009Lindsay A. Matthews The Cdc7,Dbf4 complex plays an instrumental role in the initiation of DNA replication and is a target of replication-checkpoint responses in Saccharomyces cerevisiae. Cdc7 is a conserved serine/threonine kinase whose activity depends on association with its regulatory subunit, Dbf4. A conserved sequence near the N-terminus of Dbf4 (motif N) is necessary for the interaction of Cdc7,Dbf4 with the checkpoint kinase Rad53. To understand the role of the Cdc7,Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encompassing motif N was isolated, overproduced and crystallized. A complete native data set was collected at 100,K from crystals that diffracted X-rays to 2.75,Å resolution and structure determination is currently under way. [source] Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2009Andreas Winklmeier The tetramerization domain (T1 domain) derived from the voltage-dependent potassium channel Kv1.3 of Homo sapiens was recombinantly expressed in Escherichia coli and purified. The crystals were first grown in an NMR tube in 150,mM potassium phosphate pH 6.5 in the absence of additional precipitants. The crystals showed I4 symmetry characteristic of the naturally occurring tetrameric assembly of the single subunits. A complete native data set was collected to 1.2,Å resolution at 100,K using synchrotron radiation. [source] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilisACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2009Marcus Resch The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50,Å resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit. [source] Crystallization and preliminary structure analysis of the blue laccase from the ligninolytic fungus Panus tigrinusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2005Marta Ferraroni The blue laccase from the white-rot basidiomycete fungus Panus tigrinus, an enzyme involved in lignin biodegradation, has been crystallized. P. tigrinus laccase crystals grew within one week at 296,K using the sitting-drop vapour-diffusion method in 22%(w/v) PEG 4000, 0.2,M CaCl2, 100,mM Tris,HCl pH 7.5. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.2, b = 111.6, c = 97.1, , = 97.7°, and contain 46% solvent. A complete native data set was collected to 1.4,Å resolution at the copper edge. Molecular replacement using the Coprinus cinereus laccase structure (PDB code 1hfu) as a starting model was performed and initial electron-density maps revealed the presence of a full complement of copper ions. Model refinement is in progress. The P. tigrinus laccase structural model exhibits the highest resolution available to date and will assist in further elucidation of the catalytic mechanism and electron-transfer processes for this class of enzymes. [source] | ||||||||||