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Correlation between protein stability and crystal properties of designed ROP variants
Author(s) -
Kokkinidis Michael,
Vlassi Metaxia,
Papanikolaou Yannis,
Kotsifaki Dina,
Kingswell Adrian,
Tsernoglou Demetrius,
Hinz HansJuuml;rgen
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340160208
Subject(s) - differential scanning calorimetry , crystallization , crystallography , diffraction , resolution (logic) , materials science , protein crystallization , mutant , yield (engineering) , crystal (programming language) , x ray crystallography , chemistry , physics , optics , biochemistry , thermodynamics , organic chemistry , artificial intelligence , computer science , gene , programming language , metallurgy
Six variants of the ROP protein, designed with the aim to analyze by X‐ray crystallography loop formation and core packing interactions in 4‐α‐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 resolutionX‐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. © Wiley‐Liss, Inc.