Crystallization and preliminary X-ray diffraction analysis of Langat virus envelope protein domain III.
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.
White
Mark A
MA
Sealy Center for Structural Biology, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch at Galveston, Galveston, Texas 77555-0647, USA.
Liu
Deqian
D
Holbrook
Michael R
MR
Shope
Robert E
RE
Barrett
Alan D T
AD
Fox
Robert O
RO
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
D008567:Membranes, Artificial; D014759:Viral Envelope Proteins