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Title
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Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.
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Authors
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M.Ambrazi,
G.Fellas,
E.G.Kapetaniou,
D.Kotsifaki,
M.Providaki,
M.Kokkinidis.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
432-434.
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PubMed id
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Abstract
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Rop is the paradigm of a canonical four-alpha-helical bundle. Its loop region
has attracted considerable interest because a single alanine-to-proline
substitution (A31P) in the loop is sufficient to change the topology of this
small protein. In order to further analyse the loop region as a possible
folding-control element, the double mutant D30P/A31G (RopPG) was produced,
purified and crystallized. The crystals belonged to space group P2(1), with
unit-cell parameters a = 26.7, b = 38.8, c = 56.6 A, beta = 100.9 degrees and
two molecules in the asymmetric unit. A complete data set was collected at 100 K
to a resolution of 1.4 A using synchrotron radiation.
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