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B6db references: 12777822

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 selected
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 2007/12/12 15:45

B6db references