Correlation between protein stability and crystal properties of designed ROP variants.
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.
Kokkinidis
M
M
Department of Biology, University of Crete, Greece.
Vlassi
M
M
Papanikolaou
Y
Y
Kotsifaki
D
D
Kingswell
A
A
Tsernoglou
D
D
Hinz
H J
HJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D009154:Mutation; D016601:RNA-Binding Proteins; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; C054243:Rop protein, ColE1 plasmid