title: Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirus.
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.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, C. V. Raman Avenue, Bangalore, Karnataka 560 012, India.
authors.forename: Anita R
authors.initials: AR
authors.lastname: Chacko
authors.forename: Peter H
authors.initials: PH
authors.lastname: Zwart
authors.forename: Randy J
authors.initials: RJ
authors.lastname: Read
authors.forename: Eleanor J
authors.initials: EJ
authors.lastname: Dodson
authors.forename: C D
authors.initials: CD
authors.lastname: Rao
authors.forename: Kaza
authors.initials: K
authors.lastname: Suguna
mesh_terms: D016880:Anisotropy; D018360:Crystallography, X-Ray; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D012401:Rotavirus / Q000737:chemistry*; D012400:Rotavirus Infections / Q000821:virology*; D014118:Toxins, Biological / Q000737:chemistry*; D017361:Viral Nonstructural Proteins / Q000737:chemistry*
chemical_list: D006023:Glycoproteins; C081369:NS28 protein, rotavirus; D014118:Toxins, Biological; D017361:Viral Nonstructural Proteins