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.