Purification, crystallization and preliminary X-ray investigation of the complex of human vitamin D binding protein and rabbit muscle actin

被引：7
作者：
Bogaerts, I
Verboven, C
Rabijns, A
Waelkens, E
Van Baelen, H
De Ranter, C
机构：
[1] Katholieke Univ Leuven, Fac Ciencias Wetenschappen, Lab Analyt Chem Med Fysicochem, B-3000 Louvain, Belgium
[2] Katholieke Univ Leuven, Afdeling Biochem Onderwijs Navorsing, B-3000 Louvain, Belgium
[3] Katholieke Univ Leuven, Lab Expt Geneeskunde Endocrinol Onderwijs Navorsi, B-3000 Louvain, Belgium
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷
关键词：
D O I：
10.1107/S090744490100350X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The vitamin D binding protein binds globular actin with high affinity and is involved in the clearance of actin from the blood circulation. A complex of the human vitamin D binding protein and rabbit muscle actin was subjected to purification steps. The pure complex was crystallized using the hanging-drop vapour-diffusion procedure. The best obtained crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 74.44, b = 74.90, c = 88.02 Angstrom, beta = 110.19 degrees. A complete data set to 2.4 Angstrom was collected from a single crystal using synchrotron radiation at DESY, Hamburg, Germany.
引用
收藏
页码：740 / 742
页数：3
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