Purification, crystallization and preliminary X-ray diffraction analysis of an oomycete-derived Nep1-like protein

B. Luberacki, M. Weyand, H.U. Seitz, W. Koch, C. Oecking, C. Ottmann

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Samenvatting

The elicitor protein Nep1-like protein from the plant pathogen Pythium aphanidermatum was purified and crystallized using the hanging-drop vapour-diffusion method. A native data set was collected to 1.35 angstrom resolution at 100 K using synchrotron radiation. Since selenomethionine-labelled protein did not crystallize under the original conditions, a second crystal form was identified that yielded crystals that diffracted to 2.1 angstrom resolution. A multiple-wavelength anomalous dispersion (MAD) experiment was performed at 100 K and all four selenium sites were identified, which allowed solution of the structure
Originele taal-2Engels
Pagina's (van-tot)1178-1180
TijdschriftActa crystallographica. Section F, Structural biology and crystallization communications
Volume64
Nummer van het tijdschrift12
DOI's
StatusGepubliceerd - 2008

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