The local resolution map of R-β-actin and comparison of the R-β-actin, chicken, and rabbit skeletal muscle actin structures. (A) The purified Ac- and R-actin were polymerized in vitro and ultracentrifuged at 100,000 × g for 1 h. The proteins in the supernatant (S) and pellet (P) were assessed by SDS-PAGE and Coomassie staining. (B) The local resolution map of R-β-actin color coded as per the legend. (C) Ribbon diagram comparing the structure of R-β-actin presented here (cyan) with previously published structures of chicken (navy) and rabbit (magenta) skeletal muscle actin. (D) Close-up view comparing the structure of the active site of R-β-actin with previously published structures of chicken and rabbit skeletal muscle actin. (E) Close up view comparing the N-terminal sections of R-β-actin to that of chicken and rabbit skeletal muscle actin. Source data are available for this figure: SourceData FS1.