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Title
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Purification, crystallization and preliminary X-ray diffraction analysis of an oomycete-derived Nep1-like protein.
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Authors
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B.Luberacki,
M.Weyand,
U.Seitz,
W.Koch,
C.Oecking,
C.Ottmann.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
1178-1180.
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PubMed id
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Abstract
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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 A 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 A 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.
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