Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures.
Optimum coordinate sets have been obtained for ferrocytochrome c and the two symmetry-independent molecules of ferricytochrome c from tuna at 2.0 A resolution by making the best fit of models with standard bond lengths and angles to the experimental electron density maps (1977) J. Biol. Chem. 252, 759-785, as a preliminary to full refinement with 1.5 A data. Both the Diamond model-building programs and locally developed minicomputer routines were tried, with the latter preferred for economy and ease of operation, although both gave satisfactory results. Atomic coordinates are available on microfiche or from the Brookhaven Protein Data Bank. Using the two ferricytochrome molecules as a control, no differences between oxidized and reduced cytochrome molecules can be seen that are outside the probable limits of accuracy of the 2.0 A analysis. Rotation and subtractive difference map comparisons also show no conformation changes. If believable differences do appear in the course of the 1.5 A refinement now underway, these should be no more than minor breathing of main chain or adjustment of side chains.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D003201:Computers; D003461:Crystallography; D003574:Cytochrome c Group; D005399:Fishes / Q000378:metabolism*; D006418:Heme / Q000032:analysis; D008956:Models, Chemical; D008958:Models, Molecular; D009206:Myocardium / Q000201:enzymology; D009678:Nuclear Energy; D011487:Protein Conformation; D012399:Rotation; D014413:Tuna / Q000378:metabolism*
D000596:Amino Acids; D003574:Cytochrome c Group; D006418:Heme