Open AccessIsolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus
Author(s) -
Akrem Ahmed,
Iqbal Sadaf,
Buck Friedrich,
Meyer Arne,
Perbandt Markus,
Voelter Wolfgang,
Betzel Christian
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110053698
Subject(s) - chitinase , crystallization , crystallography , chemistry , monoclinic crystal system , biology , botany , crystal structure , biochemistry , enzyme , organic chemistry
A chitinase has been isolated and purified from Crocus vernus corms. N‐terminal amino‐acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging‐drop vapour‐diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C 2, with unit‐cell parameters a = 172.3, b = 37.1, c = 126.4 Å, β = 127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1 Å.