DIFFRACTION QUALITY CRYSTALS OF PROTEIN-X FROM AZOTOBACTER-VINELANDII

Citation
Tc. Diller et al., DIFFRACTION QUALITY CRYSTALS OF PROTEIN-X FROM AZOTOBACTER-VINELANDII, Journal of Molecular Biology, 241(4), 1994, pp. 620-621
Citations number
12
Categorie Soggetti
Biology
ISSN journal
00222836
Volume
241
Issue
4
Year of publication
1994
Pages
620 - 621
Database
ISI
SICI code
0022-2836(1994)241:4<620:DQCOPF>2.0.ZU;2-Q
Abstract
Protein X from Azotobacter vinelandii has recently been shown to be ei ther a NADPH oxidase or a NADP(+) reductase that interacts specificall y with ferredoxin I. Single crystals have been obtained by vapor diffu sion from polyethylene glycol 4000 solutions containing 100 mM citrate buffer (pH 5.5). The crystals belong to space group P2(1)2(1)2 with u nit cell constants a = 68.9 Angstrom, b = 76.9 Angstrom c = 52.8 Angst rom and one molecule (M(r) 29,000) per asymmetric unit. The crystals d iffract to 2.5 Angstrom resolution.