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

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)


Interna författare/redaktörer


Publikationens författare: Nymalm Y, Kidron H, Söderholm A, Viitanen L, Kaukonen K, Pihlavisto M, Smith D, Veromaa T, Airenne TT, Johnson MS, Salminen TA
Förläggare: BLACKWELL MUNKSGAARD
Publiceringsår: 2003
Tidskrift: Acta Crystallographica Section D: Biological Crystallography
Tidskriftsakronym: ACTA CRYSTALLOGR D
Volym: 59
Artikelns första sida, sidnummer: 1288
Artikelns sista sida, sidnummer: 1290
Antal sidor: 3
ISSN: 0907-4449


Abstrakt

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%.

Senast uppdaterad 2019-08-12 vid 03:26

Dela länk