Abstract
WE have prepared deuterated bovine pancreatic ribonuclease (Armour, lot 381–059) by the procedures of Hermans and Scheraga1. Both RNaseH20 (all but 20 exchangeable H's exchanged) and RNase all-deuterated crystallized from 55 per cent (v/v) aqueous 2-methyl-2,4-pentanediol (deuterated solvent) in form II2. The intensities of the X-ray reflexions along the principal axes were identical within experimental precision to those of non-deuterated crystals out to 2θ = 60° (1.5 Å. resolution); at higher angles RNase gives poor reflexions. The lattice constants were identical to those of undeuterated crystals within the normal variation (± 0.05 Å. and ± 0.03°). The small differences between deuterium bonds and hydrogen bonds do not change the structure of RNase within the limits observable by X-ray diffraction. Detectable changes might be produced in the case of a crystallizable protein with a transition temperature near room temperature instead of the high transition temperature (61° C.) of RNase2.
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Hermans, jun., J., and Scheraga, H. A., J. Amer. Chem. Soc., 82, 5156 (1960).
King, M. V., Magdoff, B. S., Adelman, M. B., and Harker, D., Acta Cryst., 9, 460 (1956).
Harrington, W. F., and Schellman, J. A., C.R. Trav. Lab. Carlsberg, Ser. Chim., 30, 21 (1956).
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BELLO, J., HARKER, D. Crystallization of Deuterated Ribonuclease. Nature 192, 756 (1961). https://doi.org/10.1038/192756a0
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DOI: https://doi.org/10.1038/192756a0
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