Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the effector protein MoHrip1 from Magnaporthe oryzae
Author(s) -
Zhang Caizhi,
Liu Xinqi,
Qiu Dewen,
Zeng Hongmei
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113006490
Subject(s) - magnaporthe , polyethylene glycol , crystallization , cadmium chloride , chloride , nuclear chemistry , chemistry , hydrate , molecular replacement , cobalt , crystallography , cadmium , inorganic chemistry , biochemistry , organic chemistry , oryza sativa , magnaporthe grisea , gene
The effector protein MoHrip1 from the pathogenic fungus Magnaporthe oryzae was purified and crystallized using the sitting‐drop vapour‐diffusion method. Native crystals appeared in a solution composed of 0.005 M cobalt(II) chloride hexahydrate, 0.005 M nickel(II) chloride hexahydrate, 0.005 M cadmium chloride hydrate, 0.005 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 12%( w / v ) polyethylene glycol 3350. A native data set was collected to 1.9 Å resolution at 100 K using an in‐house X‐ray source. The structure of MoHrip1 was successfully determined by molecular replacement using a homologous structure.