Crystallization and X-ray analysis of bovine glycolipid transfer protein

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: West G, Nymalm Y, Airenne TT, Kidron H, Mattjus P, Salminen TT
Publiceringsår: 2004
Tidskrift: Acta Crystallographica Section D: Biological Crystallography
Tidskriftsakronym: ACTA CRYSTALLOGR D
Volym: 60
Nummer: 4
Artikelns första sida, sidnummer: 703
Artikelns sista sida, sidnummer: 705
Antal sidor: 3
ISSN: 0907-4449
eISSN: 1399-0047


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.

Senast uppdaterad 2019-15-11 vid 05:30