TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of langat virus envelope protein domain III
AU - White, Mark A.
AU - Liu, Deqian
AU - Holbrook, Michael R.
AU - Shope, Robert E.
AU - Barrett, Alan D.T.
AU - Fox, Robert O.
PY - 2003/6/1
Y1 - 2003/6/1
N2 - 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, P3121 or P3221, with unit-cell parameters a = 80.93, c = 132.1 Å and a = 104.8, c = 219.5 Å for forms I and II, respectively. Complete data sets to 2.9 and 3.35 Å, respectively, have been collected at 100 K with Cu Kα X-rays from a rotating-anode generator.
AB - 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, P3121 or P3221, with unit-cell parameters a = 80.93, c = 132.1 Å and a = 104.8, c = 219.5 Å for forms I and II, respectively. Complete data sets to 2.9 and 3.35 Å, respectively, have been collected at 100 K with Cu Kα X-rays from a rotating-anode generator.
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U2 - 10.1107/S0907444903004475
DO - 10.1107/S0907444903004475
M3 - Article
C2 - 12777770
AN - SCOPUS:0038722641
SN - 0907-4449
VL - 59
SP - 1049
EP - 1051
JO - Acta Crystallographica - Section D Biological Crystallography
JF - Acta Crystallographica - Section D Biological Crystallography
IS - 6
ER -