Purification, crystallization and preliminary X-ray diffraction analysis of the effector protein MoHrip1 from Magnaporthe oryzae.

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. [ABSTRACT FROM AUTHOR]