6533b7d2fe1ef96bd125e18b
RESEARCH PRODUCT
Production, crystallization and preliminary X-ray analysis of the human integrin alpha1 I domain.
Jyrki HeinoJyrki HeinoYvonne NymalmMark S. JohnsonTiina A. SalminenJarmo KäpyläJussi Kankaresubject
biologyProtein ConformationRecombinant Fusion ProteinsIntegrinIntegrin alpha1General MedicineCrystallography X-Raylaw.inventionCollagen receptorchemistry.chemical_compoundCrystallographychemistryStructural BiologylawAntigens CDDomain (ring theory)PEG ratioGlycerolbiology.proteinHumansCrystallizationCrystallizationSingle crystalSodium acetatedescription
Integrin α1β1 is one of the main collagen receptors in many cell types. A fast large-scale production, purification and crystallization method for the integrin α1 I domain is reported here. The α1 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 Å, α = γ = 90.0, β = 90.8°. The crystals diffract to 2.0 Å and a 94.2% complete data set to 2.2 Å has been collected from a single crystal with an R merge of 5.8%.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-07-07 | Acta crystallographica. Section D, Biological crystallography |