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Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1020-2.

Crystallization and preliminary X-ray analysis of the beta-isoform of glutamate decarboxylase from Escherichia coli.

Author information

1
Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

Abstract

Glutamate decarboxylase (GAD) is a vitamin B6 enzyme which catalyzes the alpha-decarboxylation of L-glutamate to gamma-aminobutyric acid (GABA). Escherichia coli cells coexpress two highly homologous enzyme isoforms, GADalpha and GADbeta. Well diffracting crystals of GADbeta were obtained by taking advantage of the possibility of expressing each isoform separately. They belong to space group P31 or P32 with the unit-cell dimensions a = b = 115.6 and c = 206.6 A and contain one GAD hexamer in the asymmetric unit. High-resolution synchrotron data were collected at 100 K for the native protein and a potential heavy-atom derivative.

PMID:
9757126
DOI:
10.1107/s0907444998003497
[Indexed for MEDLINE]

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