Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis

@article{Perutz1960StructureOH,
  title={Structure of H{\ae}moglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis},
  author={Max Ferdinand Perutz and Michael G. Rossmann and Ann F. Cullis and Hilary Muirhead and George Will and A. C. North},
  journal={Nature},
  year={1960},
  volume={185},
  pages={416-422}
}
Structure Of Hæemoglobin: A Three-Dimensional Fourier Synthesis of Reduced Human Haemoglobin at 5.5 Å Resolution
Structure Of Haeemoglobin: A Three-Dimensional Fourier Synthesis of Reduced Human Haemoglobin at 5.5 A Resolution
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Identification of the Black Sub-Unit of the Crystallographic Model of Horse Hæmoglobin with the Valyl-Glutaminyl Polypeptide Chain
THE three-dimensional Fourier synthesis of horse hæmoglobin showed four sub-units which were identical in pairs1. In the model of the molecule, these two kinds of sub-units were painted black and
Three-dimensional structure of human serum albumin.
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TLDR
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It was in 1912, at the University of Munich, that Friedrich and Knipping, following a suggestion from Max von Laue, produced the first X-ray diffraction pattern by irradiating a single crystal of ZnS
X-ray diffraction studies of immunoglobulins.
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