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Crystallization and diffraction to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein
A Spyridaki1, N M Glykos, D Kotsifaki
1Institute of Molecular Biology and Biotechnology (IMBB), PO Box 1527, GR-71110 Heraklion, Crete, Greece.
Acta Crystallographica. Section D, Biological Crystallography
|August 16, 2000
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.