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

doi:10.1107/S1744309110041515

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 journal › Article › Research › peer-review

18 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	1572-1578
Number of pages	7
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	12
DOIs	https://doi.org/10.1107/S1744309110041515
Publication status	Published - Dec 2010
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1107/S1744309110041515

Cite this

@article{6047a9500b1e49c8b6f457150b920a03,

title = "A new crystal form of human vascular adhesion protein 1",

abstract = "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 {\AA}, Β = 112.3°. The structure was refined to a resolution of 2.9 {\AA}, with R cryst and R free values of 0.250 and 0.286, respectively.",

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

year = "2010",

month = dec,

doi = "10.1107/S1744309110041515",

language = "English",

volume = "66",

pages = "1572--1578",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "International Union of Crystallography",

number = "12",

}

TY - JOUR

T1 - A new crystal form of human vascular adhesion protein 1

AU - Ernberg, Karin

AU - McGrath, Aaron P.

AU - Peat, Thomas S.

AU - Adams, Timothy E.

AU - Xiao, Xiaowen

AU - Pham, Tam

AU - Newman, Janet

AU - McDonald, Ian A.

AU - Collyer, Charles A.

AU - Guss, J. Mitchell

PY - 2010/12

Y1 - 2010/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=78650110702&partnerID=8YFLogxK

U2 - 10.1107/S1744309110041515

DO - 10.1107/S1744309110041515

M3 - Article

C2 - 21139198

AN - SCOPUS:78650110702

SN - 1744-3091

VL - 66

SP - 1572

EP - 1578

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 12

ER -

A new crystal form of human vascular adhesion protein 1

Abstract

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this