Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans

被引:5
作者
Evrard, C [1 ]
Declercq, JP [1 ]
Fastrez, J [1 ]
机构
[1] UNIV CATHOLIQUE LOUVAIN, LAB BIOCHIM PHYS & BIOPOLYMERES, B-1348 LOUVAIN, BELGIUM
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1997年 / 53卷
关键词
D O I
10.1107/S0907444996011523
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
After many unsuccessful attempts to crystallize the bacteriophage lambda lysozyme, a mutant where all the tryptophan residues have been replaced by aza-tryptophans has been crystallized by the vapor-diffusion method. The crystals are orthorhombic and belong to space group P2(1)2(1)2(1) With cell dimensions a = 73.01, b = 78.80, c = 82.31 Angstrom. Diffraction data were collected using synchrotron radiation sources. Crystals diffract to a resolution of 2.3 Angstrom. Data from two different platinum derivatives were also recorded to 2.8 and 2.5 Angstrom, respectively.
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收藏
页码:217 / 219
页数:3
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