CRYSTALLIZATION OF EUKARYOTIC E3, LIPOAMIDE DEHYDROGENASE, FROM YEAST, FOR EXHIBITING X-RAY-DIFFRACTION BEYOND 2.5 ANGSTROM RESOLUTION, ANDPRELIMINARY STRUCTURE-ANALYSIS

Citation
T. Toyoda et al., CRYSTALLIZATION OF EUKARYOTIC E3, LIPOAMIDE DEHYDROGENASE, FROM YEAST, FOR EXHIBITING X-RAY-DIFFRACTION BEYOND 2.5 ANGSTROM RESOLUTION, ANDPRELIMINARY STRUCTURE-ANALYSIS, Journal of Biochemistry, 121(1), 1997, pp. 1-4
Citations number
20
Categorie Soggetti
Biology
Journal title
ISSN journal
0021924X
Volume
121
Issue
1
Year of publication
1997
Pages
1 - 4
Database
ISI
SICI code
0021-924X(1997)121:1<1:COEELD>2.0.ZU;2-J
Abstract
Lipoamide dehydrogenase, which is a common component of alpha-keto aci d dehydrogenase complexes, has been highly purified from yeast (Saccha romyces cerevisiae) to reveal its structure at higher resolution, New crystals obtained by a desalting method exhibited diffraction beyond 2 .5 Angstrom resolution, The cell dimensions are a = 97.1, b = 158.7, a nd c = 67.9 Angstrom, and the space group is P2(1)2(1)2(1). There is a dimeric enzyme in the asymmetric unit, The crystal structure was solv ed by means of the molecular-replacement technique and refined in a pr eliminary manner.