Crystallization and X-ray analysis of bovine glycolipid transfer protein

被引：16

作者：

West, G ^{[1
]}

Nymalm, Y ^{[1
]}

Airenne, TT ^{[1
]}

Kidron, H ^{[1
]}

Mattjus, P ^{[1
]}

Salminen, TT ^{[1
]}

机构：

[1] Abo Akad Univ, Dept Biochem & Pharm, FIN-20521 Turku, Finland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S090744490400109X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glycolipid-transfer protein (GLTP) is a 24 kDa basic cytosolic protein that facilitates the transfer of glycolipids between bilayer membranes in vitro, but its in vivo function is unknown. Human, bovine, porcine and murine GLTPs have recently been cloned and share high sequence identity to each other. The three-dimensional structure of GLTP has not yet been solved and no structures of any proteins related to GLTP are known. Therefore, the structure of GLTP might reveal a currently unknown fold. Here, the crystallization and preliminary X-ray analysis of bovine GLTP are reported for the first time. Protein prepared by recombinant techniques using an Escherichia coli expression system has been crystallized using the vapour-diffusion method. The crystals belong to space group P2(1), with unit-cell parameters a=55.4, b=34.9, c=58.5 Angstrom, alpha=gamma=90, beta=116degrees. The crystals diffract to 1.6 Angstrom resolution and a 97.1% complete data set with an R-merge of 6.7% has been collected from a single crystal at 100 K using synchrotron radiation.

引用

页码：703 / 705

页数：3

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