Abstract
THE importance of water of crystallization in maintaining the regular structure of protein crystals has already been shown in the X-ray examination of wet and dry crystals of three different proteins: lactoglobulin, hæmoglobin and chymotrypsin1. It is now possible to add insulin to this list. Although the original photographs2 of air-dried insulin crystals recorded no X-ray reflections with spacings smaller than 7 A., those of the wet crystals examined in their mother-liquor show reflections with spacings of 2·4 A. or less, which indicate that here there is regularity in the structure down to atomic dimensions.
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References
Crowfoot, D., Riley, D., Bernal, J. D., Fankuchen, I., and Perutz, M. NATURE, 141, 521 (1938).
Crowfoot, D., Proc. Roy. Soc., A, 164, 580 (1938).
Bernal, J. D., Proe. Roy. Soc., B, 127, 36 (1939).
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CROWFOOT, D., RILEY, D. X-Ray Measurements on Wet Insulin Crystals. Nature 144, 1011–1012 (1939). https://doi.org/10.1038/1441011a0
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DOI: https://doi.org/10.1038/1441011a0
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