Abstract
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
| Original language | English |
|---|---|
| Pages (from-to) | 1178-1180 |
| Journal | Acta crystallographica. Section F, Structural biology and crystallization communications |
| Volume | 64 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2008 |
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Luberacki, B., Weyand, M., Seitz, H. U., Koch, W., Oecking, C., & Ottmann, C. (2008). Purification, crystallization and preliminary X-ray diffraction analysis of an oomycete-derived Nep1-like protein. Acta crystallographica. Section F, Structural biology and crystallization communications, 64(12), 1178-1180. https://doi.org/10.1107/S1744309108037640