Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1.
Alkaline phosphatases (APs) are widely distributed from microbes to humans and are involved in several important biological processes such as phosphate nutrition, signal transduction and pathogenesis. Alkaline phosphatases are also useful in various industrial applications and in recombinant DNA technology. A new AP enzyme from Sphingomonas sp. strain BSAR-1, termed PhoK, has been shown to be useful in uranium bioprecipitation. PhoK was expressed, purified and crystallized. The crystals belonged to space group P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 87.37, c = 168.16 A, and contained one enzyme molecule in the asymmetric unit. Native diffraction data have been collected to 1.95 A resolution at the ESRF.
Nilgiriwala
Kayzad S
KS
Molecular Biology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India.
Bihani
Subhash C
SC
Das
Amit
A
Prashar
Vishal
V
Kumar
Mukesh
M
Ferrer
Jean Luc
JL
Apte
Shree Kumar
SK
Hosur
M V
MV
D000469:Alkaline Phosphatase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005110:Extracellular Space / Q000201:enzymology*; D020578:Sphingomonas / Q000201:enzymology*
D001426:Bacterial Proteins; D000469:Alkaline Phosphatase