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Article

Crystallization and diffraction to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein.

Acta crystallographica. Section D, Biological crystallography - 1 Aug 2000

Spyridaki A, Glykos N M, Kotsifaki D, Fadouloglou V E, Kokkinidis M

Abstract excerpt

The Rop protein is the paradigm of a highly regular four-alpha-helix bundle and as such has been subject to numerous structural and mutagenesis studies. Crystals of a designed Rop variant which establishes a continuous heptad pattern through the bend region have been obtained by a combination of vapour-diffusion and seeding techniques. The crystals diffract to ultrahigh (0.8 A) resolution using synchrotron...

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Identifiers

PMID: 10944340
DOI: 10.1107/s0907444900006296

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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