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

doi:10.1107/s0907444999006009

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 journal › Article › Scientific › peer-review

15 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 language	Undefined/Unknown
Pages (from-to)	1365–1367
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
DOIs	https://doi.org/10.1107/s0907444999006009
Publication status	Published - 1999
MoE publication type	A1 Journal article-refereed

Access to Document

10.1107/s0907444999006009

Cite this

@article{f5e973ed02684f0ea19ec764dab0cc96,

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

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\%.",

author = "Tiina Salminen and Yvonne Nymalm and J. Kankare and J. K{\"a}pyl{\"a} and J. Heino and Johnson, \{Mark S\}",

year = "1999",

doi = "10.1107/s0907444999006009",

language = "Odefinierat/ok{\"a}nt",

volume = "55",

pages = "1365–1367",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "Wiley",

}

TY - JOUR

T1 - Production, crystallization and preliminary X-ray analysis of the human integrin alpha(1) I domain

AU - Salminen, Tiina

AU - Nymalm, Yvonne

AU - Kankare, J.

AU - Käpylä, J.

AU - Heino, J.

AU - Johnson, Mark S

PY - 1999

Y1 - 1999

N2 - 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%.

AB - 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%.

U2 - 10.1107/s0907444999006009

DO - 10.1107/s0907444999006009

M3 - Artikel

SN - 0907-4449

VL - 55

SP - 1365

EP - 1367

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

ER -