2aut
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(New page: 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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Revision as of 06:15, 21 November 2007
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Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium
Overview
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 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.
Reference
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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