Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the effector protein PevD1 from Verticillium dahliae
Author(s) -
Han Lei,
Liu Zheng,
Liu Xinqi,
Qiu Dewen
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112020556
Subject(s) - verticillium dahliae , crystallization , iodine , chemistry , resolution (logic) , sodium formate , analytical chemistry (journal) , crystallography , materials science , biology , chromatography , botany , inorganic chemistry , organic chemistry , artificial intelligence , computer science
The effector protein PevD1 from the pathogenic fungus Verticillium dahliae was purified and crystallized using the hanging‐drop vapour‐diffusion method. Native crystals appeared in a solution consisting of 4.0 M sodium formate. A native data set was collected at 1.9 Å resolution at 100 K using an in‐house X‐ray source. Because of the absence of useful methinione in the protein sequence, derivative crystals that contained iodine were obtained by soaking in 1.25 M potassium iodide, and a data set that contained anomalous signal was collected using the same X‐ray facility at a wavelength of 1.54 Å. The single‐wavelength anomalous dispersion method was used to successfully solve the structure based on the anomalous signal generated from iodine.