Literature DB >> 10393790

Production, crystallization and preliminary X-ray analysis of the human integrin alpha1 I domain.

T A Salminen1, Y Nymalm, J Kankare, J Käpylä, J Heino, M S Johnson.   

Abstract

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%.

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Year:  1999        PMID: 10393790     DOI: 10.1107/s0907444999006009

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Structure of collagen receptor integrin α(1)I domain carrying the activating mutation E317A.

Authors:  Matti Lahti; Eva Bligt; Henri Niskanen; Vimal Parkash; Anna-Maria Brandt; Johanna Jokinen; Pekka Patrikainen; Jarmo Käpylä; Jyrki Heino; Tiina A Salminen
Journal:  J Biol Chem       Date:  2011-10-26       Impact factor: 5.157

2.  Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.

Authors:  Ana Monica Nunes; Jie Zhu; Jacqueline Jezioro; Conceição A S A Minetti; David P Remeta; Richard W Farndale; Samir W Hamaia; Jean Baum
Journal:  Protein Sci       Date:  2016-08-01       Impact factor: 6.725

  2 in total

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