BARC/PUB/2003/0002

 
 

Purification, crystallization and preliminary X-ray diffraction studies of recombinant class A non-specific acid phosphatase of Salmonella typhimurium

 
     
 
Author(s)

Makde, R. D.; Vinay Kumar; Rao, A. S.; Yadava, V. S.; Mahajan, S. K.
(SRS;MB&AD;SSPD)

Source

Acta Crystallographica - D, 2003. Vol. 59 (3): pp. 515-518

ABSTRACT

The phoN gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK-.The nucleotide sequence of the cloned gene differs from the corre-sponding S. typhimurium LT2 sequence at 23 residues, leading to 15 amino-acid differences, but was very close to the S. typhi phoN sequence (only three nucleotide and two amino-acid differences).The recombinant PhoN protein was purified to homogeneity. Two forms of crystals were harvested from a single crystallization condition. Diffraction intensity data were collected using a laboratory X-ray source to resolution limits of 2.5 and 2.8 Â for crystals belonging to space group C2 and C 2221, respectively. Based on non-crystallographic symmetry, four monomers of PhoN are expected to be present in the asymmetric unit of the C2 unit cell. Two monomers of a biologically active dimer in the asymmetric unit of the C2221 unit cell are expected from the Matthews coefficient.

 
 
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