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

Yvonne Nymalm, H Kidron, A Söderholm, L Viitanen, K Kaukonen, M Pihlavisto, D Smith, T Veromaa, Tomi Airenne, Mark S Johnson, Tiina Salminen

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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%.
Original languageUndefined/Unknown
Pages (from-to)1288–1290
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Publication statusPublished - 2003
MoE publication typeA1 Journal article-refereed

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