Orientation of histidine residues in RNase A: neutron diffraction study.
- 1 May 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (5) , 2853-2855
- https://doi.org/10.1073/pnas.78.5.2853
Abstract
Difference Fourier maps were calculated at 2.8 .ANG. resolution by using neutron diffraction data obtained from a single crystal of [bovine pancreatic] RNase A. The phases were derived from a model resulting from the joint refinement of X-ray and neutron data at 2.0 .ANG. and 2.8 .ANG. resolution, respectively. The orientation of histidine-48 assumed during the refinement of the X-ray model at 2.5 .ANG. was confirmed, whereas the other 3 histidines had to be rotated around C.beta.-C.gamma. bonds to agree with the neutron difference Fourier maps. In the final model, histidine-12 is clearly hydrogen bonded to the carbonyl oxygen of threonine-45 and to the O2 of the inorganic phosphate, and histidine-119 is bonded to another O2 of the phosphate and to the oxygen OD1 of aspartic acid 121.This publication has 9 references indexed in Scilit:
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