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Crystallization and preliminary diffraction data for iso-1-cytochrome c from yeast.

C Sherwood, G D Brayer

    Journal of Molecular Biology
    |September 5, 1985
    PubMed
    Summary
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    Researchers crystallized yeast iso-1-cytochrome c, an electron transfer protein, enabling detailed structural analysis. This work also produced crystals of key mutants for studying the electron transport chain.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Iso-1-cytochrome c is a crucial electron transfer protein in yeast (Saccharomyces cerevisiae).
    • Understanding its structure is vital for elucidating the electron transport chain.
    • Previous structural data may be limited for specific mutants.

    Purpose of the Study:

    • To obtain high-quality crystals of yeast iso-1-cytochrome c for structural determination.
    • To crystallize and characterize mutants of iso-1-cytochrome c, particularly at the Phe87 residue.
    • To facilitate detailed structural and functional analysis of electron transfer mechanisms.

    Main Methods:

    • Protein crystallization using ammonium sulfate precipitation from a buffered solution.
    • X-ray diffraction analysis to determine crystal space group and unit cell dimensions.

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  • Characterization of crystal stability and diffraction resolution.

    • Main Results:

    • Successfully obtained deep red crystals of yeast iso-1-cytochrome c.
    • Determined crystal space group as P4(1)2(1)2 (or P4(3)2(1)2) with specific unit cell parameters.
    • Crystals exhibited stability in X-ray beams and diffracted to better than 2.0 A resolution.
    • Obtained morphologically similar crystals of three Phe87 mutants of iso-1-cytochrome c.

    Conclusions:

    • The crystallization of wild-type and mutant iso-1-cytochrome c provides a foundation for high-resolution structural studies.
    • These crystal forms are suitable for X-ray crystallography, enabling detailed structural insights.
    • The structural data will advance the understanding of the electron transport chain and the role of Phe87.