Crystallization and preliminary X-ray crystallographic analysis of d-phenylglycine aminotransferase from Pseudomonas stutzeri ST201.
Acta Crystallogr D Biol Crystallogr
; 59(Pt 5): 953-4, 2003 May.
Article
em En
| MEDLINE
| ID: mdl-12777822
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.
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Base de dados:
MEDLINE
Assunto principal:
Pseudomonas stutzeri
/
Transaminases
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article