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Purification, Crystallization and Preliminary X-ray Diffraction Analysis of the Effector Protein MoHrip1 From Magnaporthe Oryzae

Purification, Crystallization and Preliminary X-ray Diffraction Analysis of the Effector Protein MoHrip1 From Magnaporthe Oryzae

Caizhi Zhang, Xinqi Liu, Dewen Qiu, Hongmei Zeng

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):460-2.

PMID: 23545660

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP69098142	Cobalt(II) chloride hydrate		69098-14-2	Price

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