Purification, crystallization and preliminary X‐ray diffraction analysis of the effector protein MoHrip1 from  Magnaporthe oryzae | Zendy

Zhang Caizhi | Zendy; Liu Xinqi | Zendy; Qiu Dewen | Zendy; Zeng Hongmei | Zendy

Open Access

Purification, 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.

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