title: Crystallization and preliminary X-ray diffraction analysis of Langat virus envelope protein domain III.
abstract: The putative receptor-binding domain (domain III) of the flavivirus Langat envelope glycoprotein has been crystallized using the hanging-drop vapor-diffusion method at 277 K. Two distinct crystal morphologies were observed to grow under the same conditions. The crystal forms both belong to a trigonal space group, P3(1)21 or P3(2)21, with unit-cell parameters a = 80.93, c = 132.1 A and a = 104.8, c = 219.5 A for forms I and II, respectively. Complete data sets to 2.9 and 3.35 A, respectively, have been collected at 100 K with Cu Kalpha X-rays from a rotating-anode generator.
authors.affiliation: Sealy Center for Structural Biology, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston, Galveston, Texas 77555-0647, USA.
authors.forename: Mark A
authors.initials: MA
authors.lastname: White
authors.forename: Deqian
authors.initials: D
authors.lastname: Liu
authors.forename: Michael R
authors.initials: MR
authors.lastname: Holbrook
authors.forename: Robert E
authors.initials: RE
authors.lastname: Shope
authors.forename: Alan D T
authors.initials: AD
authors.lastname: Barrett
authors.forename: Robert O
authors.initials: RO
authors.lastname: Fox
mesh_terms: D002850:Chromatography, Gel; D003460:Crystallization; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D008567:Membranes, Artificial; D010957:Plasmids / Q000737:chemistry; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D008567:Membranes, Artificial; D014759:Viral Envelope Proteins