Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Makde RD, Kumar V, Gupta GD, Jasti J, Singh TP, Mahajan SK. Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1849-52. Epub 2003, Sep 19. PMID:14501135
