Crystallization and X-ray analysis of bovine glycolipid transfer protein

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: West G, Nymalm Y, Airenne TT, Kidron H, Mattjus P, Salminen TT
Publication year: 2004
Journal: Acta Crystallographica Section D: Biological Crystallography
Journal acronym: ACTA CRYSTALLOGR D
Volume number: 60
Issue number: 4
Start page: 703
End page: 705
Number of pages: 3
ISSN: 0907-4449
eISSN: 1399-0047


Abstract

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.

Last updated on 2019-23-09 at 03:31