Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
