Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirus.
Acta Crystallogr D Biol Crystallogr
; 68(Pt 11): 1541-8, 2012 Nov.
Article
en En
| MEDLINE
| ID: mdl-23090403
ABSTRACT
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 Å. Severe diffraction anisotropy, rotational pseudosymmetry 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.
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Bases de datos:
MEDLINE
Asunto principal:
Infecciones por Rotavirus
/
Toxinas Biológicas
/
Glicoproteínas
/
Proteínas no Estructurales Virales
/
Rotavirus
Límite:
Humans
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2012
Tipo del documento:
Article
País de afiliación:
India