title: Correlation between protein stability and crystal properties of designed ROP variants.
abstract: Six variants of the ROP protein, designed with the aim to analyze by X-ray crystallography loop formation and core packing interactions in 4-alpha-helical bundles, have been purified and a search of their crystallization conditions has been carried out. Five mutants yield crystals that are suitable for medium to high resolution X-ray diffraction studies. For all mutants crystal size, sensitivity to X-irradiation and diffraction limit are correlated to their stability as determined by differential scanning calorimetry, in a manner which is not yet understood in detail.
authors.affiliation: Department of Biology, University of Crete, Greece.
authors.forename: M
authors.initials: M
authors.lastname: Kokkinidis
authors.forename: M
authors.initials: M
authors.lastname: Vlassi
authors.forename: Y
authors.initials: Y
authors.lastname: Papanikolaou
authors.forename: D
authors.initials: D
authors.lastname: Kotsifaki
authors.forename: A
authors.initials: A
authors.lastname: Kingswell
authors.forename: D
authors.initials: D
authors.lastname: Tsernoglou
authors.forename: H J
authors.initials: HJ
authors.lastname: Hinz
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D009154:Mutation; D016601:RNA-Binding Proteins; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid