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

Tiina Salminen, Yvonne Nymalm, J. Kankare, J. Käpylä, J. Heino, Mark S Johnson

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

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%.
Original languageUndefined/Unknown
Pages (from-to)1365–1367
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
DOIs
Publication statusPublished - 1999
MoE publication typeA1 Journal article-refereed

Cite this