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Crystallization and preliminary diffraction data for horse heart metmyoglobin.

C Sherwood, A G Mauk, G D Brayer

    Journal of Molecular Biology
    |January 5, 1987
    PubMed
    Summary

    Researchers crystallized horse heart metmyoglobin, yielding reddish-brown crystals. Similar crystal forms were achieved for myoglobin derivatives with modified heme groups, aiding structural studies.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Metmyoglobin is a form of myoglobin where the iron in the heme group is oxidized.
    • Understanding the structure of metmyoglobin is crucial for elucidating its function and interactions.

    Purpose of the Study:

    • To obtain well-ordered crystals of horse heart metmyoglobin suitable for X-ray diffraction analysis.
    • To investigate the crystallization behavior of horse heart myoglobin derivatives with modified heme prosthetic groups.

    Main Methods:

    • Crystallization of metmyoglobin using hanging drop and batch methods.
    • X-ray diffraction analysis of obtained crystals.
    • Preparation and crystallization of myoglobin derivatives with altered heme groups.

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    Main Results:

    • Reddish-brown crystals of horse heart metmyoglobin were successfully obtained in space group P2(1).
    • Crystallographic data: a = 64.3 A, b = 28.9 A, c = 35.9 A, beta = 107.1 degrees.
    • Morphologically similar crystal forms were achieved for three horse heart myoglobin derivatives with modified heme groups.

    Conclusions:

    • The crystallization methods employed are effective for obtaining horse heart metmyoglobin crystals.
    • The structural integrity of myoglobin is maintained in its metmyoglobin form and with modified heme groups, allowing for structural studies.