title: Purification, crystallization and preliminary X-ray diffraction analysis of an oomycete-derived Nep1-like protein.
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 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.
authors.affiliation: Center for Plant Molecular Biology, Auf der Morgenstelle 5, 72076 Tübingen, Universität Tübingen, Germany.
authors.forename: Borries
authors.initials: B
authors.lastname: Luberacki
authors.forename: Michael
authors.initials: M
authors.lastname: Weyand
authors.forename: Ulrich
authors.initials: U
authors.lastname: Seitz
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Koch
authors.forename: Claudia
authors.initials: C
authors.lastname: Oecking
authors.forename: Christian
authors.initials: C
authors.lastname: Ottmann
mesh_terms: D020418:Algal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D011775:Pythium / Q000378:metabolism*; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D020418:Algal Proteins; D012645:Selenomethionine