Production, crystallization and preliminary X-ray analysis of the human integrin alpha(1) I domain

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: T. A. Salminen, Y. Nymalm, J. Kankare, J. Käpylä, J. Heino and M. S. Johnson
Publication year: 1999
Journal: Acta Crystallographica Section D: Biological Crystallography
Journal acronym: ACTA CRYSTALLOGR D
Volume number: 55
Start page: 1365
End page: 1367
Number of pages: 3
ISSN: 0907-4449


Integrin alpha(1)beta(1) is one of the main collagen receptors in many cell types. A fast large-scale production, purification and crystallization method for the integrin alpha(1) I domain is reported here. The alpha(1) I domain was crystallized using the vapour-diffusion method with a reservoir solution containing a mixture of PEG 4000, sodium acetate, glycerol and Tris-HCl buffer. The crystals beong to the C2 space group, with unit-cell parameters a = 74.5, b = 81.9, c = 37.3 Angstrom, alpha = gamma = 90.0, beta = 90.8 degrees. The crystals diffract to 2.0 K and a 94.2% complete data set to 2.2 Angstrom has been collected from a single crystal with an R-merge of 5.8%.

Last updated on 2020-14-07 at 07:02