Summary
X-ray studies on semi-synthetic human insulin have shown that it crystallizes in the rhombohedral space group R3 and is nearly isomorphous with 2 Zn pig insulin. Precession photographs of crystals of human and pig insulins show observable changes in the intensity patterns. Crystallographic analysis and refinement of semi-synthetic human insulin at 1.9 Å resolution have shown that its molecular structure is very like that of pig insulin except at the C-terminus of the B chain where the change in sequence occurs. We also report the results of a high resolution crystallographic study of human insulins from different origins. The X-ray diffraction patterns of three non-pancreatic human insulins are indistinguishable from each other and from pancreatic human insulin. Refinement of the structures of the non-pancreatic human insulins has shown that they are identical within the limits of experimental error.
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The determination of the human (semi-synthetic) 2 Zn insulin structure was carried out at the University of York. The part of the paper in which the human 2 Zn insulin crystal structures from different origins are compared was carried out at Birkbeck College (London) and the University of York.
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Chawdhury, S.A., Dodson, E.J., Dodson, G.G. et al. The crystal structures of three non-pancreatic human insulins. Diabetologia 25, 460–464 (1983). https://doi.org/10.1007/BF00284451
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DOI: https://doi.org/10.1007/BF00284451