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Rotating-anode X-ray Source (rotating-anode + x-ray_source)
Selected AbstractsPreliminary crystallographic study of Thermus aquaticus glycerol kinaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2001Hua-Shan Huang Glycerol kinase (GlpK) is an important enzyme which catalyzes the rate-limiting step in a central biochemical pathway involving glycerol metabolism. GlpK from the thermophile Thermus aquaticus has been overexpressed in glpK -deficient Escherichia coli and crystallized by the hanging-drop method. The crystal belongs to the cubic space group I23, with unit-cell parameters a = b = c = 163.94,(3),Å. Native data were collected to 2.87,Å resolution on a Cu,K, rotating-anode X-ray source. [source] Crystallization and preliminary X-ray crystallographic studies of recombinant human betaine,homocysteine S-methyltransferaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2001Nandita Bose Betaine,homocysteine S-methyltransferase (BHMT) catalyzes a reaction essential for regulation of methionine and homocysteine metabolism and the catabolism of choline in mammalian tissues. Human recombinant BHMT (MW = 45,kDa) has been crystallized by the hanging-drop vapor-diffusion method at 294,K using ethylene glycol as the precipitant. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 109.190, b = 91.319, c = 88.661,Å, , = 122.044°, and diffract to 2.9,Å resolution on a local rotating-anode X-ray source. Rotation-function analysis and the Matthews coefficient, VM = 2.46,Å3,Da,1, are consistent with a dimer in the asymmetric unit, suggesting that the active enzyme is a tetramer with 222 symmetry. [source] Expression, purification, crystallization and preliminary X-ray analysis of the native class C ,-lactamase from Enterobacter cloacae 908R and two mutantsACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2001J. Wouters Crystals have been obtained of the Enterobacter cloacae 908R ,-lactamase and two point mutants by the vapour-diffusion method using similar conditions [pH 9.0, polyethylene glycol (Mr = 6000) as precipitant]. The three crystal forms belong to the orthorhombic space group P21212, with roughly the same unit-cell parameters; i.e. for the wild-type crystals a = 46.46, b = 82.96, c = 95.31,Å. In the best cases, the crystals diffract to about 2.1,Å resolution on a rotating-anode X-ray source at room temperature. Co-crystallization experiments of poor substrates with the wild-type protein and the active-site serine mutant (S64C) are planned and should lead to a better understanding of the catalytic mechanism of class C ,-lactamases. [source] Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thalianaACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2010Zhu-Bing Shi VSP1 is a defence protein in Arabidopsis thaliana that may also be involved in control of plant development. The recombinant protein has been overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to 1.9,Å resolution and a complete X-ray data set was collected at 100,K using Cu,K, radiation from a rotating-anode X-ray source. The crystals belonged to space group C2. As there are no related structures that could be used as a search model for molecular replacement, work is in progress on experimental phasing using heavy-atom derivatives and selenomethionine derivatives. [source] Purification, crystallization and preliminary crystallographic studies on 2-dehydro-3-deoxygalactarate aldolase from Leptospira interrogansACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2006Xu Li 2-Dehydro-3-deoxygalactarate (DDG) aldolase is a member of the class II aldolase family and plays an important role in the pyruvate-metabolism pathway, catalyzing the reversible aldol cleavage of DDG to pyruvate and tartronic semialdehyde. As it is a potential novel antibiotic target, it is necessary to elucidate the catalytic mechanism of DDG aldolase. To determine the crystal structure, crystals of DDG aldolase from Leptospira interrogans were obtained by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.2,Å resolution using a Cu,K, rotating-anode X-ray source. The crystal belonged to space group C2, with unit-cell parameters a = 293.5, b = 125.6, c = 87.6,Å, , = 100.9°. The VM is calculated to be 2.4,Å3,Da,1, assuming there to be 12 protein molecules in the asymmetric unit. [source] Isolation, crystallization and preliminary X-ray analysis of a methanol-induced corrinoid protein from Moorella thermoaceticaACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2005Weihong Zhou A corrinoid protein was induced and overexpressed in methanol-grown cells of the thermophilic anaerobic bacterium Moorella thermoacetica. The protein was purified from cytosolic extracts. After screening for crystallization conditions and optimization, crystals were obtained that diffracted strongly on a rotating-anode X-ray source. A diffraction data set was collected and processed including reflections to 1.9,Å resolution. Reflections were indexed in a primitive orthorhombic cell with unit-cell parameters a = 55.69, b = 62.74, c = 34.54,Å. N-terminal amino-acid sequencing indicates that the crystals contain a C-terminal fragment of the protein. [source] | ||||||||||