CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE BETA-ISOFORM OFGLUTAMATE-DECARBOXYLASE FROM ESCHERICHIA-COLI

Authors
MALASHKEVICH VN DEBIASE D MARKOVICHOUSLEY Z SCHLUNEGGER MP BOSSA F JANSONIUS JN
Citation
Vn. Malashkevich et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE BETA-ISOFORM OFGLUTAMATE-DECARBOXYLASE FROM ESCHERICHIA-COLI, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 1020-1022
Citations number
17
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
5
Pages
1020 - 1022
Database
ISI
SICI code
0907-4449(1998)54:<1020:CAPAOT>2.0.ZU;2-E
Abstract
Glutamate decarboxylase (GAD) is a vitamin B-6 enzyme which catalyzes the alpha-decarboxylation of L-glutamate to gamma-aminobutyric acid (G ABA). Escherichia coli cells coexpress two highly homologous enzyme is oforms, GAD alpha and GAD beta. Well diffracting crystals of GAD beta were obtained by taking advantage of the possibility of expressing eac h isoform separately. They belong to space group P3(1) or P3(2) with t he unit-cell dimensions a = b = 115.6 and c = 206.6 Angstrom and conta in one GAD hexamer in the asymmetric unit. High-resolution synchrotron data were collected at 100 K for the native protein and a potential h eavy-atom derivative.