Crystallization and preliminary x-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1

Abstract

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 P4₃2₁2 or P4₁2₁2, 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.