Temperature-dependent X-ray diffraction as a probe of protein structural dynamics
- 1 August 1979
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 280 (5723) , 558-563
- https://doi.org/10.1038/280558a0
Abstract
X-ray diffraction at 4 temperatures from 220-300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1261 non-hydrogen atoms of metmyoglobin. Results indicate a condensed core around the heme, semi-liquid regions towards the outside and a possible pathway for ligands. X-ray diffraction can provide the spatial distribution of the dynamic features of a protein.This publication has 28 references indexed in Scilit:
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