Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirus
Data(s) |
01/11/2012
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Resumo |
The crystal structure of the region spanning residues 95-146 of the rotavirus nonstructural protein NSP4 from the asymptomatic human strain ST3 was determined at a resolution of 2.5 angstrom. Severe diffraction anisotropy, rotational pseudo-symmetry and twinning complicated the refinement of this structure. A systematic explanation confirming the crystal pathologies and describing how the structure was successfully refined is given in this report. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/45367/1/acta_cry_D_68-11_cha_2012.pdf Chacko, Anita R and Zwart, Peter H and Read, Randy J and Dodson, Eleanor J and Rao, CD and Suguna, Kaza (2012) Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirus. In: Acta Crystallographica Section D Biological Crystallography, 68 (11). pp. 1541-1548. |
Publicador |
International Union of Crystallography |
Relação |
http://dx.doi.org/10.1107/S090744491203836X http://eprints.iisc.ernet.in/45367/ |
Palavras-Chave | #Molecular Biophysics Unit #Microbiology & Cell Biology |
Tipo |
Journal Article PeerReviewed |