CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF A NADH OXIDASE FROM THERMUS-THERMOPHILUS HB8

被引：7
|
作者：
ERDMANN, H [1 ]
HECHT, HJ [1 ]
PARK, HJ [1 ]
SPRINZL, M [1 ]
SCHOMBURG, D [1 ]
SCHMID, RD [1 ]
机构：
[1] UNIV BAYREUTH,BIOCHEM LAB,W-8580 BAYREUTH,GERMANY
来源：
JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 230卷 / 03期
关键词：
NADH OXIDASE; THERMUS-THERMOPHILUS; CRYSTALLIZATION; X-RAY DIFFRACTION; FAD;
D O I：
10.1006/jmbi.1993.1222
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The thermophile NADH oxidase from Thermus thermophilus, cloned and expressed in Escherichia coli, has been purified to homogeneity and crystallized. Three different crystal forms were found to be suitable for X-ray diffraction analysis. Crystals of the tetragonal form, grown in the presence of 25% polyethylene glycol 4000 and 0.25 M-NaCl at pH 6.6, were chosen for further analysis. These crystals belong to the space group P41(3)212 with refined lattice constants of a = 94.8 Å and c = 49.0 Å, indicating a cell content of one monomer per asymmetric unit of the crystal. The crystals diffract to a resolution of 2.2 Å. © 1993 Academic Press, Inc.
引用
收藏
页码：1086 / 1088
页数：3
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