A new crystal form of human vascular adhesion protein 1

Karin Ernberg, Aaron P. McGrath, Thomas S. Peat, Timothy E. Adams, Xiaowen Xiao, Tam Pham, Janet Newman, Ian A. McDonald, Charles A. Collyer, J. Mitchell Guss

Research output: Contribution to journalArticleResearchpeer-review

18 Citations (Scopus)


Human vascular adhesion protein 1 (VAP-1) is involved in lymphocyte-endothelial cell adhesion and has been implicated in many human inflammatory diseases. VAP-1 is a member of the copper amine oxidase family of enzymes with a trihydroxyphenylalanine quinone (TPQ) cofactor. Previously characterized crystals of VAP-1 suffered from anisotropy and contained disordered regions; in addition, one form was consistently twinned. In an effort to grow crystals that diffracted to higher resolution for inhibitor-binding studies, a construct with an N-terminal deletion was made and expressed in the Chinese hamster ovary (CHO) glycosylation mutant cell line Lec8. Screening produced crystals that displayed some anisotropy and contained seven molecules per asymmetric unit. These crystals belonged to space group C2, with unit-cell parameters a = 394.5, b = 115.8, c = 179.3 Å, Β = 112.3°. The structure was refined to a resolution of 2.9 Å, with R cryst and R free values of 0.250 and 0.286, respectively.

Original languageEnglish
Pages (from-to)1572-1578
Number of pages7
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number12
Publication statusPublished - Dec 2010
Externally publishedYes


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