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The expression, purification, crystallization and data collection and processing of the effector protein MoHrip1 from M. oryzae are reported.

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A novel effector protein was recombinantly expressed, purified and crystallized. The structure was solved using the selenium SAD method.

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The GRASP65 GRASP domain from R. norvegicus has been expressed, purified and crystallized. The crystals belonged to space group P21212, with unit-cell parameters a = 44.99, b = 104.29, c = 37.93 Å, and diffracted to 2.0 Å resolution.

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The deaminase AmnE from Pseudomonas sp. AP-3 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for this recombinant enzyme.

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