type	Journal Article
authors	Kongsaeree P, Samanchart C, Laowanapiban P, Wiyakrutta S, Meevootisom V.
title	Crystallization and preliminary X-ray crystallographic analysis of d-phenylglycine aminotransferase from Pseudomonas stutzeri ST201
journal	Acta Crystallogr D Biol Crystallogr
Activity	2.6.1.72
Family	2.6.1.72
sel	unselected
ui	12777822
year	(2003)
volume	59
pages	953-4
keywords	Base Sequence
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 P3(1)21 or P3(2)21, with unit-cell parameters a = b = 75.155, c = 147.554 A. 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 A.
last changed	2017/07/24 13:58