title: Purification, crystallization and preliminary X-ray diffraction analysis of the effector protein PevD1 from Verticillium dahliae.
abstract: 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.
authors: Key Laboratory of Integrated Pest Management in Crops, Ministry of Agriculture, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, 12 Zhongguancun South Street, Beijing 100081, People's Republic of China.
authors: Lei
authors: L
authors: Han
authors: Zheng
authors: Z
authors: Liu
authors: Xinqi
authors: X
authors: Liu
authors: Dewen
authors: D
authors: Qiu
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D020172:Verticillium / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins