Correlation between protein stability and crystal properties of designed ROP variants
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Updated: Oct 17, 2026

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
M Kokkinidis1, M Vlassi, Y Papanikolaou
1Department of Biology, University of Crete, Greece.
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.
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