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%.
|Julkaisu||Acta Crystallographica Section D: Biological Crystallography|
|DOI - pysyväislinkit|
|Tila||Julkaistu - 2003|
|OKM-julkaisutyyppi||A1 Julkaistu artikkeli, soviteltu|