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Crystallization and X-Ray Analysis of Rhodothermus marinus Cytochrome c at 1.23 Å Resolution

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Abstract:

Cytochrome c from Rhodothermus marinus has been crystallized using the hanging-drop vapor-diffusion method in 30 % (w/v) polyethylene glycol 8K, 0.2 M ammonium sulfate, 8 % hexanediol and 50 mM sodium citrate pH 2.2. The crystals belong to space group P21. X-ray diffraction data were collected to 1.23 Å resolution using synchrotron radiation and a wavelength of 0.93 Å.





Keywords: Cytochrome c; Rhodothermus marinus; crystallization; thermophiles

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607782541024

Publication date: 2007-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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