title: X-ray diffraction analysis of glycoprotein D from herpes simplex virus type 2.
abstract: Glycoprotein D (gD) of Herpes simplex virus type 2 (HSV-2) is a key factor mediating the entry of HSV-2 into host cells. In order to explain the mechanism underlying the gD-mediated receptor-binding and viral entry, we performed a structural study on HSV-2 gD. The ectodomain of the gD protein encompassing residues 1 to 285 was expressed by baculovirus-infected insect cells as a secreted soluble protein with a C-terminal hexa-his tag. The protein was then purified by affinity and size-exclusion chromatography. The purified protein was successfully crystallized using the hanging-drop vapor-diffusion at 18 degrees C in a condition consisting of 0.1 mol/L Hepes pH 7.2, 5% (V/V) 2-methyl-2,4-pentanediol (MPD) and 10% PEG 10 000. The crystals diffracted to 1.8 angstroms resolution and belonged to space group P21, with unit-cell parameters alpha = 63.6, b = 55.4, c = 65.3 angstroms, beta = 96.3 degrees.
authors.affiliation: College of Life Science, Anhui Agricultural University, Hefei 230036, China.
authors.forename: Zhujun
authors.initials: Z
authors.lastname: Chen
authors.forename: Guangwen
authors.initials: G
authors.lastname: Lu
authors.forename: Jianxun
authors.initials: J
authors.lastname: Qi
authors.forename: Xiang
authors.initials: X
authors.lastname: Xu
authors.forename: Na
authors.initials: N
authors.lastname: Zhang
authors.forename: Jinghua
authors.initials: J
authors.lastname: Yan
authors.forename: Rongfu
authors.initials: R
authors.lastname: Wang
mesh_terms: D000818:Animals; D016367:Baculoviridae; D003460:Crystallization; D018360:Crystallography, X-Ray; D018258:Herpesvirus 2, Human / Q000737:chemistry*; D007313:Insecta / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D014760:Viral Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D014760:Viral Fusion Proteins