Crystallization and preliminary X-ray analysis of the human vascular adhesion protein-1

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Nymalm Y, Kidron H, Söderholm A, Viitanen L, Kaukonen K, Pihlavisto M, Smith D, Veromaa T, Airenne TT, Johnson MS, Salminen TA
Publisher: BLACKWELL MUNKSGAARD
Publication year: 2003
Journal: Acta Crystallographica Section D: Biological Crystallography
Journal acronym: ACTA CRYSTALLOGR D
Volume number: 59
Start page: 1288
End page: 1290
Number of pages: 3
ISSN: 0907-4449


Abstract

Human vascular adhesion protein-1 (VAP-1) is a membrane-bound multifunctional glycoprotein with both adhesive and enzymatic properties. The protein belongs to the copper-containing amine oxidase (CAO) family, which use 2,4,5-trihydroxyphenylalanine quinone as a cofactor. Here, the crystallization and preliminary X-ray analysis of a mammalian CAO, human VAP-1, is reported. The protein was expressed in Chinese hamster ovary cells as a full-length form with an N-terminal transmembrane region and multiple glycosylation sites. Hexagonal crystals with unit-cell parameters a=b=225.9, c=218.7 Angstrom, alpha=beta=90, gamma=120degrees were obtained using the vapour-diffusion method. Data from three different crystals were collected at 100 K using synchrotron radiation and were processed to 3.2 Angstrom resolution with 95.9% completeness and an R-merge of 19.6%.

Last updated on 2019-16-10 at 02:35