4do2 | pdb_00004do2
From Proteopedia
Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
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Structural highlights
Publication Abstract from PubMedRop 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. Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein.,Ambrazi M, Fellas G, Kapetaniou EG, Kotsifaki D, Providaki M, Kokkinidis M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):432-4. doi:, 10.1107/S1744309108011342. Epub 2008 Apr 30. PMID:18453719[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 17:13, 9 December 2014.