Abstract
X-ray diffraction data have been collected from four isomorphous crystalline derivatives of the proteolytic enzyme elastase, and a map of the three-dimensional electron density of the tosyl derivative has been calculated by Fourier synthesis of 2,750 independent terms. It shows clearly the conformation of the elastase polypeptide chain, the size and orientation of the amino-acid side-chains, and the position of the tosyl group which labels the active centre of the enzyme.
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WATSON, H., SHOTTON, D., COX, J. et al. Three-dimensional Fourier Synthesis of Tosyl-elastase at 3.5 Å Resolution. Nature 225, 806–811 (1970). https://doi.org/10.1038/225806a0
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DOI: https://doi.org/10.1038/225806a0
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