Crystallization and preliminary X-ray crystallographic analysis of D-phenylglycine aminotransferase from Pseudornonas stutzeri ST201

Abstract

D-Phenylglycine aminotransferase (D-PhgAT) catalyzes the reversible transamination of D-phenylglycine to L-glutamate with 2-oxoglutarate as the amino-group acceptor. Crystals of substrate-free Pseudomonas stutzeri D-PhgAT bound to the cofactor pyridoxal-5′-phosphate (PLP) were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 75.155, c = 147.554 Å. The asymmetric unit contains one molecule of D-PhgAT and has a solvent content of 50.0%. A complete native X-ray diffraction data set was collected from a single crystal at 100 K to a resolution of 2.3 Å.