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

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

doi:10.1107/s0907444900006296

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

Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):1015-6. doi: 10.1107/s0907444900006296.

Authors

A Spyridaki¹, N M Glykos, D Kotsifaki, V E Fadouloglou, M Kokkinidis

Affiliation

¹ Institute of Molecular Biology and Biotechnology (IMBB), PO Box 1527, GR-71110 Heraklion, Crete, Greece.

PMID: 10944340
DOI: 10.1107/s0907444900006296

Abstract

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 radiation and cryogenic conditions.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Crystallization
Crystallography, X-Ray
Escherichia coli / chemistry
Escherichia coli / genetics
Genetic Variation
Mutagenesis, Site-Directed

Substances

Bacterial Proteins