TY  - JOUR
AU  - Scott, SA
AU  - Holloway, G
AU  - Coulson, BS
AU  - Szyczew, AJ
AU  - Kiefel, MJ
AU  - von Itzstein, M
AU  - Blanchard, H
Y2  - 2014/05/21
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y2  - 2005/05/03
Y1  - 2005/06/01
SN  - 1744-3091
UR  - http://hdl.handle.net/11343/26407
AB  - Rotavirus recognition and attachment to host cells involves interaction with the spike protein VP4 that projects outwards from the surface of the virus particle. An integral component of these spikes is the VP8* domain, which is implicated in the direct recognition and binding of sialic acid-containing cell-surface carbohydrates and facilitates subsequent invasion by the virus. The expression, purification, crystallization and preliminary X-ray diffraction analysis of VP8* from porcine CRW-8 rotavirus is reported. Diffraction data have been collected to 2.3 A resolution, enabling the determination of the VP8* structure by molecular replacement.
N1  - application/pdf
LA  - English
PB  - INT UNION CRYSTALLOGRAPHY
KW  - Medical Virology ; Infectious Diseases
T1  - Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8
DO  - 10.1107/S1744309105013849
IS  - ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
VL  - 61
IS  - Pt 6
SP  - 617-620
L1  - /bitstream/handle/11343/26407/116203_5247.pdf?sequence=1&isAllowed=n
ER  -