Temperature-dependent X-ray diffraction as a probe of protein structural dynamics.
X-ray diffraction at four temperatures from 220 to 300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1,261 non-hydrogen atoms of metmyoglobin. The results are interpreted to indicate a condensed core around the haem, semi-liquid regions towards the outside and a possible pathway for ligands. It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein.
D000818:Animals; D005290:Ferric Compounds; D009038:Motion; D009211:Myoglobin; D011487:Protein Conformation; D013696:Temperature; D014961:X-Ray Diffraction / Q000379:methods*
D005290:Ferric Compounds; D009211:Myoglobin