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Purification, crystallization and preliminary X-ray diffraction analysis of effector protein MoHrip2 from Magnaporthe oryzae.

ABSTRACT: MoHrip2, a novel effector protein from the pathogenic fungus Magnaporthe oryzae, was purified and crystallized using the sitting-drop vapour-diffusion method. Native crystals and selenomethionine-labelled crystals were obtained using 2.2 M ammonium sulfate as a precipitant. A native data set was collected to 2.0 Å resolution at 100 K using an in-house X-ray source and a selenomethionine-labelled data set containing anomalous signal was collected to 1.8 Å resolution at 100 K using a synchrotron source. Based on the anomalous signal generated from the Se atom, the MoHrip2 structure was successfully solved using the single-wavelength anomalous dispersion (SAD) method.

SUBMITTER: Liu M

PROVIDER: S-EPMC3614180 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction analysis of effector protein MoHrip2 from Magnaporthe oryzae.

Liu Mengjie M Liu Xinqi X Zeng Hongmei H Qiu Dewen D

Acta crystallographica. Section F, Structural biology and crystallization communications 20130329 Pt 4

MoHrip2, a novel effector protein from the pathogenic fungus Magnaporthe oryzae, was purified and crystallized using the sitting-drop vapour-diffusion method. Native crystals and selenomethionine-labelled crystals were obtained using 2.2 M ammonium sulfate as a precipitant. A native data set was collected to 2.0 Å resolution at 100 K using an in-house X-ray source and a selenomethionine-labelled data set containing anomalous signal was collected to 1.8 Å resolution at 100 K using a synchrotron s ...[more]

PMID: 23545661

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