Open AccessIsolation, crystallization and preliminary X‐ray diffraction analysis of l ‐amino‐acid oxidase from Vipera ammodytes ammodytes venom
Author(s) -
Georgieva Dessislava,
Kardas Anna,
Buck Friedrich,
Perbandt Markus,
Betzel Christian
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108027036
Subject(s) - venom , isolation (microbiology) , chemistry , crystallization , x ray , crystallography , biochemistry , biology , organic chemistry , physics , microbiology and biotechnology , optics
l ‐Amino‐acid oxidase from the venom of Vipera ammodytes ammodytes , the most venomous snake in Europe, was isolated and crystallized using the sitting‐drop vapour‐diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C 2, with unit‐cell parameters a = 198.37, b = 96.38, c = 109.11 Å, β = 92.56°. Initial diffraction data were collected to 2.6 Å resolution. The calculated Matthews coefficient is approximately 2.6 Å 3 Da −1 assuming the presence of four molecules in the asymmetric unit.