Crystallization and diffraction to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein.
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.
Spyridaki
A
A
Institute of Molecular Biology and Biotechnology (IMBB), PO Box 1527, GR-71110 Heraklion, Crete, Greece.
Glykos
N M
NM
Kotsifaki
D
D
Fadouloglou
V E
VE
Kokkinidis
M
M
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D014644:Genetic Variation; D016297:Mutagenesis, Site-Directed
D001426:Bacterial Proteins