Open AccessCrystallization and preliminary X‐ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR‐1
Author(s) -
Nilgiriwala Kayzad S.,
Bihani Subhash C.,
Das Amit,
Prashar Vishal,
Kumar Mukesh,
Ferrer JeanLuc,
Apte Shree Kumar,
Hosur M. V.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109031133
Subject(s) - alkaline phosphatase , crystallization , phosphatase , enzyme , extracellular , resolution (logic) , recombinant dna , chemistry , strain (injury) , biology , crystallography , biochemistry , anatomy , gene , organic chemistry , computer science , artificial intelligence
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 P 4 3 2 1 2 or P 4 1 2 1 2, with unit‐cell parameters a = b = 87.37, c = 168.16 Å, and contained one enzyme molecule in the asymmetric unit. Native diffraction data have been collected to 1.95 Å resolution at the ESRF.