Crystallization and preliminary X-ray analysis of β-alanine synthase from the yeast Saccharomyces kluyveri

被引:5
作者
Dobritzsch, D [1 ]
Gojkovic, Z
Andersen, B
Piskur, J
机构
[1] Karolinska Inst, Dept Biochem Med, Stockholm, Sweden
[2] Tech Univ Denmark, BioCentrum DTU, DK-2800 Lyngby, Denmark
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444903009120
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In eukaryotes and some bacteria, the third step of reductive pyrimidine catabolism is catalyzed by beta-alanine synthase (EC 3.5.1.6). Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri were obtained using sodium citrate as a precipitant. The crystals belong to space group P2(1) (unit-cell parameters a=117.2, b=77.1, c=225.5 Angstrom, beta=95.0degrees) and contain four homodimers per asymmetric unit. Data were collected to 2.7 Angstrom resolution. Introduction of heavy atoms into the crystal lattice induced a different set of unit-cell parameters (a=61.0, b=77.9, c=110.1 Angstrom, beta=97.2degrees) in the same space group P2(1), with only one homodimer per asymmetric unit.
引用
收藏
页码:1267 / 1269
页数:3
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