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Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution : (I) X-ray Analysis

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Abstract

The phase angles of 8,000 reflexions were determined by the method of isomorphous replacement, using crystals of native haemoglobin and of three heavy atom derivatives. The electron density maps show the positions of nearly all the amino-acid residues and some details of the haem groups. Next week the second part of this article—the atomic model—will appear.

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Author notes

  1. F. S. MATHEWS

    Present address: Department of Physiology, Washington University, St Louis, USA

  2. E. L. McGANDY

    Present address: Department of Biochemistry and Nutrition, University of Pittsburgh, USA

  3. L. E. WEBB

    Present address: Department of Chemistry, Illinois Institute of Technology, Chicago, USA

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge

    M. F. PERUTZ, H. MUIRHEAD, J. M. COX, L. C. G. GOAMAN, F. S. MATHEWS, E. L. McGANDY & L. E. WEBB

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  1. M. F. PERUTZ
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  2. H. MUIRHEAD
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  3. J. M. COX
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  4. L. C. G. GOAMAN
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  5. F. S. MATHEWS
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  6. E. L. McGANDY
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  7. L. E. WEBB
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PERUTZ, M., MUIRHEAD, H., COX, J. et al. Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution : (I) X-ray Analysis. Nature 219, 29–32 (1968). https://doi.org/10.1038/219029a0

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  • DOI: https://doi.org/10.1038/219029a0

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