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Purification, crystallization and preliminary X-ray diffraction analysis of the effector protein MoHrip1 from Magnaporthe oryzae.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Apr2013, Vol. 69 Issue 4, p460-462. 3p. - Publication Year :
- 2013
-
Abstract
- 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]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 69
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 86641734
- Full Text :
- https://doi.org/10.1107/S1744309113006490