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Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase
Ylianttila, MS ; Qin, YM ; Hiltunen, JK ; Glumoff, T
刊名生物化学与生物物理学研究通讯
2004
关键词17 beta-HSD MFE-2 beta-oxidation peroxisome SDR PEROXISOMAL MULTIFUNCTIONAL ENZYME BIFUNCTIONAL PROTEIN-DEFICIENCY BETA-OXIDATION RAT-LIVER CRYSTAL-STRUCTURE HYDROXYSTEROID DEHYDROGENASE RESOLUTION FAMILY ACID SDR
DOI10.1016/j.bbrc.2004.09.013
英文摘要The N-terminal part of Candida tropicalis MFE-2 (MFE-2(h2Delta)) having two (3R)-hydroxyacyl-CoA dehydrogenases with different substrate specificities has been purified and crystallized as a recombinant protein. The expressed construct was modified so that a stabile. homogeneous protein could be obtained instead of an unstabile wild-type form with a large amount of cleavage products. Cubic crystals with unit cell parameters a = 74.895, b = 78.340, c = 95.445, and alpha = beta = gamma = 90degrees were obtained by using PEG 4000 as a precipitant. The crystals exhibit the space group P2(1)2(1)2(1) and contain one molecule, consisting of two different (3R)-hydroxyacyl-CoA dehydrogenases, in the asymmetric unit. The crystals diffract to a resolution of 2.2 Angstrom at a conventional X-ray source. (C) 2004 Elsevier Inc. All rights reserved.; Biochemistry & Molecular Biology; Biophysics; SCI(E); 0; ARTICLE; 1; 25-30; 324
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/254618]  
专题生命科学学院
推荐引用方式
GB/T 7714
Ylianttila, MS,Qin, YM,Hiltunen, JK,et al. Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase[J]. 生物化学与生物物理学研究通讯,2004.
APA Ylianttila, MS,Qin, YM,Hiltunen, JK,&Glumoff, T.(2004).Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase.生物化学与生物物理学研究通讯.
MLA Ylianttila, MS,et al."Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase".生物化学与生物物理学研究通讯 (2004).
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