2aut

Revision as of 09:15, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2aut" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aut, resolution 2.25Å" /> '''Crystal structure of...)
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Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium

File:2aut.jpg


2aut, resolution 2.25Å

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OverviewOverview

The aphA gene of Salmonella enterica sv. Typhimurium strain MD6001 was, cloned in the multicopy plasmid pBluescript SK(-). The recombinant AphA, protein was purified to homogeneity. The protein crystallized in the, orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a =, 112.4, b = 130.2, c = 139.6 A. Consistent with the self-rotation function, there are two tetramers in the asymmetric unit, indicating a solvent, content of approximately 54%. The crystals are composed of biologically, active AphA molecules.

About this StructureAbout this Structure

2AUT is a Single protein structure of sequence from Salmonella typhimurium with MG, NA and PO4 as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.

ReferenceReference

Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium., Makde RD, Kumar V, Gupta GD, Jasti J, Singh TP, Mahajan SK, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1849-52. Epub 2003, Sep 19. PMID:14501135

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