Production, crystallization and preliminary X-ray analysis of the human integrin alpha1 I domain.
Integrin alpha1beta1 is one of the main collagen receptors in many cell types. A fast large-scale production, purification and crystallization method for the integrin alpha1 I domain is reported here. The alpha1 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 belong to the C2 space group, with unit-cell parameters a = 74.5, b = 81.9, c = 37.3 A, alpha = gamma = 90.0, beta = 90.8 degrees. The crystals diffract to 2.0 A and a 94.2% complete data set to 2.2 A has been collected from a single crystal with an Rmerge of 5.8%.
Department of Biochemistry and Pharmacy, Abo Akademi University, PO Box 66, FIN-20521 Turku, Finland. tiina.salminen@abo.fi
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Salminen
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Nymalm
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Kankare
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Käpylä
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Heino
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Johnson
D015703:Antigens, CD / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D039423:Integrin alpha1; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics
D015703:Antigens, CD; D039423:Integrin alpha1; D011993:Recombinant Fusion Proteins