Primitive Monoclinic Space Group P21 (primitive + monoclinic_space_group_p21)

Distribution by Scientific Domains


Selected Abstracts


Expression, crystallization and preliminary X-ray crystallographic studies of Klebsiella pneumoniae maltohexaose-producing ,-amylase

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 12-2 2004
Mitsuru Momma
A recombinant form of Klebsiella pneumoniae maltohexaose-producing ,-amylase has been overexpressed in Escherichia coli and purified to homogeneity. Crystals were obtained at 293,K by the microbatch technique using 80,mM sodium/potassium phosphate buffer pH 6.2 containing 8% polyethylene glycol 3000, 4% polyethylene glycol 3350 and 40,mM sodium thiocyanate. Crystals of the overexpressed recombinant enzyme diffracted to better than 2.5, resolution at 95,K using a synchrotron-radiation source. The crystals belong to the primitive monoclinic space group P21, with unit-cell parameters a = 74.8, b = 107.6, c = 82.2,, , = 96.2. Assuming the presence of two molecules per asymmetric unit, the VM value for the crystal was 2.3,3,Da,1, indicating a solvent content of 47%. [source]


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

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2004
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, resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P21. [source]


Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009
Marc Bailly
Thermus thermophilus deprived of asparagine synthetase synthesizes Asn on tRNAAsnvia a tRNA-dependent pathway involving a nondiscriminating aspartyl-tRNA synthetase that charges Asp onto tRNAAsn prior to conversion of the Asp to Asn by GatCAB, a tRNA-dependent amidotransferase. This pathway also constitutes the route of Asn-tRNAAsn formation by bacteria and archaea deprived of asparaginyl-tRNA synthetase. The partners involved in tRNA-dependent Asn formation in T. thermophilus assemble into a ternary complex called the transamidosome. This particule produces Asn-tRNAAsn in the presence of free Asp, ATP and an amido-group donor. Crystals of the transamidosome from T. thermophilus were obtained in the presence of PEG 4000 in MES,NaOH buffer pH 6.5. They belonged to the primitive monoclinic space group P21, with unit-cell parameters a = 115.9, b = 214.0, c = 127.8,, , = 93.3. A complete data set was collected to 3, resolution. Here, the isolation and crystallization of the transamidosome from T. thermophilus and preliminary crystallographic data are reported. [source]


Crystallization and crystallographic analysis of Bacillus subtilis xylanase C

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2009
Franz J. St John
The recent biochemical characterization of the xylanases of glycosyl hydrolase family 5 (GH 5) has identified a distinctive endo mode of action, hydrolyzing the ,-1,4 xylan chain at a specific site directed by the position of an ,-1,2-linked glucuronate moiety. Xylanase C (XynC), the GH 5 xylanase from Bacillus subtilis 168, has been cloned, overexpressed and crystallized. Initial data collection was performed and a preliminary model has been built into a low-quality 2.7, resolution density map. The crystals belonged to the primitive monoclinic space group P21. Further screening identified an additive that resulted in large reproducible crystals. This larger more robust crystal form belonged to space group P21212 and a resulting data set has been processed to 1.64, resolution. This will be the second structure to be solved from this unique xylanase family and the first from a Gram-positive bacterium. This work may help to identify the structural determinants that allow the exceptional specificity of this enzyme and the role it plays in the biological depolymerization and processing of glucuronoxylan. [source]


Crystallization and preliminary X-ray diffraction analysis of the , subunit Yke2 of the Gim complex from Saccharomyces cerevisiae

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2008
Rebeca Prez de Diego
The Gim complex (GimC) from Saccharomyces cerevisiae is a heterohexameric protein complex, also known as prefoldin (PFD), which binds and stabilizes unfolded target polypeptides and subsequently delivers them to chaperonins for completion of folding. In this study, the crystallization and preliminary X-ray analysis of one of the , subunits of the Gim complex (Yke2) from S. cerevisiae are described. The purified protein was crystallized by the vapour-diffusion method, producing two types of crystals that belonged to the orthorhombic space group C222 or the primitive monoclinic space group P21. The unit-cell parameters for the C -centred orthorhombic crystal were a = 48.2, b = 168.86, c = 131.81, and the unit-cell parameters for the primitive monoclinic crystal were a = 47.83, b = 134.90, c = 81.50,, , = 100.71. The Yke2 crystals diffracted to 4.2 and 3.1, resolution, respectively, on a rotating-anode generator under cryoconditions. This is the first report concerning the crystallization of a , subunit of a eukaryotic prefoldin. [source]