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Title
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Correlation between protein stability and crystal properties of designed ROP variants.
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Authors
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M.Kokkinidis,
M.Vlassi,
Y.Papanikolaou,
D.Kotsifaki,
A.Kingswell,
D.Tsernoglou,
H.J.Hinz.
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Ref.
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Proteins, 1993,
16,
214-216.
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PubMed id
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Abstract
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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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