|
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 |
|