Send to:

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):460-2. doi: 10.1107/S1744309113006490. Epub 2013 Mar 28.

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

Author information

  • 1Key Laboratory of Integrated Pest Management in Crops, Ministry of Agriculture, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, 12 Zhongguancun South Street, Beijing 100081, People's Republic of China.


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.


Magnaporthe oryzae; MoHrip1

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for International Union of Crystallography Icon for PubMed Central
    Loading ...
    Write to the Help Desk