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

页码：740 / 742

页数：3

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