Open AccessCrystallization of a truncated soluble human semicarbazide‐sensitive amine oxidase
Author(s) -
Jakobsson Emma,
Nilsson Joakim,
Källström Ulla,
Ogg Derek,
Kleywegt Gerard J.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002678
Subject(s) - semicarbazide , crystallization , amine oxidase , amine gas treating , chemistry , organic chemistry
Human semicarbazide‐sensitive amine oxidase (SSAO) is a homodimeric copper‐containing monoamine oxidase that occurs in both a membrane‐bound and a soluble form. SSAO is also known as vascular adhesion protein‐1 (VAP‐1). A truncated soluble form of human SSAO (comprising residues 29–763) was expressed in human embryonic kidney 293 cells and purified to homogeneity. Tetragonal crystals were obtained and a data set extending to 2.5 Å was collected. The crystals are merohedrally twinned and the estimation of the twinning fraction was complicated by pseudo‐symmetry and the anisotropic character of the crystals. Using a recently developed method for twinning detection that is insensitive to phenomena such as anisotropy or pseudo‐symmetry [Padilla & Yeates (2003), Acta Cryst. D 59 , 1124–1130], the twinning fraction was estimated to be 0.3. The structure was eventually solved by molecular replacement in space group P 4 3 .