Crystallization and preliminary X-ray analysis of the human vascular adhesion protein-1.
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 A, alpha = beta = 90, gamma = 120 degrees 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 A resolution with 95.9% completeness and an R(merge) of 19.6%.
Nymalm
Yvonne
Y
Department of Biochemistry and Pharmacy, Abo Akademi University, PO Box 66, FIN-20521 Turku, Finland.
Kidron
Heidi
H
Söderholm
Annu
A
Viitanen
Lenita
L
Kaukonen
Kimmo
K
Pihlavisto
Marjo
M
Smith
David
D
Veromaa
Timo
T
Airenne
Tomi T
TT
Johnson
Mark S
MS
Salminen
Tiina A
TA
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry* / Q000302:isolation & purification; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D006031:Glycosylation; D006801:Humans; D011994:Recombinant Proteins; D014961:X-Ray Diffraction
D015815:Cell Adhesion Molecules; D011994:Recombinant Proteins; C076668:AOC3 protein, human; D006631:Amine Oxidase (Copper-Containing)