2pc5: Difference between revisions
New page: left|200px<br /><applet load="2pc5" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pc5, resolution 2.20Å" /> '''Native crystal struc... |
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==Overview== | ==Overview== | ||
The deoxyuridine triphosphate nucleotidohydrolase gene from Arabidopsis | The deoxyuridine triphosphate nucleotidohydrolase gene from Arabidopsis thaliana was expressed and the gene product was purified. Crystallization was performed by the hanging-drop vapour-diffusion method at 298 K using 2 M ammonium sulfate as the precipitant. X-ray diffraction data were collected to 2.2 A resolution using Cu K alpha radiation. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 69.90, b = 70.86 A, c = 75.55 A. Assuming the presence of a trimer in the asymmetric unit, the solvent content was 30%, with a V(M) of 1.8 A3 Da(-1). | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: magnesium]] | [[Category: magnesium]] | ||
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Revision as of 19:28, 21 February 2008
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Native crystal structure analysis on Arabidopsis dUTPase
OverviewOverview
The deoxyuridine triphosphate nucleotidohydrolase gene from Arabidopsis thaliana was expressed and the gene product was purified. Crystallization was performed by the hanging-drop vapour-diffusion method at 298 K using 2 M ammonium sulfate as the precipitant. X-ray diffraction data were collected to 2.2 A resolution using Cu K alpha radiation. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 69.90, b = 70.86 A, c = 75.55 A. Assuming the presence of a trimer in the asymmetric unit, the solvent content was 30%, with a V(M) of 1.8 A3 Da(-1).
About this StructureAbout this Structure
2PC5 is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Active as dUTP diphosphatase, with EC number 3.6.1.23 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana., Bajaj M, Moriyama H, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt, 5):409-11. Epub 2007 Apr 14. PMID:17565183
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