Flexibility within myosin heads revealed by negative stain and single- particle analysis

Journal of Cell Biology

Volumn 139, Issue 3, 1997, Pages 675-681

  Burgess, S A ^a   Walker, M L ^a   White, H D ^b   Trinick, J ^a,c  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b EASTERN VIRGINIA MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

ACTIN MYOSIN INTERACTION; ANALYTIC METHOD; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; IMAGE ANALYSIS; MUSCLE FORCE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; RABBIT; SIGNAL NOISE RATIO;

ANIMALS; CHICKENS; IMAGE PROCESSING, COMPUTER-ASSISTED; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MYOSIN SUBFRAGMENTS; MYOSINS; PARTICLE SIZE; PROTEIN STRUCTURE, TERTIARY; RABBITS; STAINING AND LABELING;

EID: 0030678623     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.3.675     Document Type: Article

References (24)

1. 2+-regulated myosin. J. Mol. Biol. 140:35-55.
2. Frank, J. 1990. Classification of macromolecular assemblies studied as "single particles." Rev. Biophys. 23:281-329.
3. Frank, J. 1996. Three-Dimensional Electron Microscopy of Macromolecular Assemblies. Academic Press, San Diego. 342 pp.
4. Frank, J., B. Shimkin, and H. Dowse. 1981a. SPIDER - a modular software system for electron image-processing. Ultramicroscopy. 6:343-357.
5. Frank, J., A. Verschoor, and M. Boublik. 1981b. Computer averaging of electron-micrographs of 40s ribosomal-subunits. Science (Wash. DC). 214:1353-1355.
6. Huxley, H.E. 1969. The mechanism of muscle contraction. Science (Wash. DC). 164:1356-1366.
7. Huxley, A.F., and R.M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature (Lond.). 233:533-538.
8. Irving, M., T. St Claire Alien, C. Sabido-David, J.S. Craik, B. Brandmeier, J. Kendrick-Jones, J.E.T. Corrie, D.R. Trentham, and Y.E. Goldman. 1995. Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature (Lond.). 375:688-691.
9. Jontes, J.D., E.M. Wilson-Kubalek, and R.A. Milligan. 1995. A 32-degrees tail swine in brush-border myosin-I on ADP release. Nature (Lond.). 378:751-753.
10. Milligan, R.A., and P.F. Flicker. 1987. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105:29-39.
11. Penczek, P., M. Radermacher, and J. Frank. 1992. 3-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy. 40:33-53.
12. Penczek, P.A., R.A. Grassucci, and J. Frank. 1994. The ribosome at improved resolution: new techniques for merging and orientation refinement in 3d cryoelectron microscopy of biological particles. Ultramicroscopy. 53:251-270.
13. Perry, S.V. 1955. Methods Enzymol. 2:582-588.
14. Rayment, I., H.M. Holden, M. Whittaker, C.B. Yohn, M. Lorenz, K.C. Holmes, and R.A. Milligan. 1993a. Structure of the actin-myosin complex and its implications for muscle contraction. Science (Wash. DC). 261:58-65.
15. Rayment, I., W.R. Rypniewski, K. Schmidtbase, R. Smith, D.R. Tomchick, M.M. Benning, D.A. Winkelmann, G. Wesenberg, and H.M. Holden. 1993b. 3-dimensional structure of myosin subfragment-1: a molecular motor. Science (Wash. DC). 261:50-58.
16. Schmitz, H., M.C. Reedy, M.K. Reedy, R.T. Tregear, H. Winkler, and K.A. Taylor. 1996. Electron tomography of insect flight-muscle in rigor and AMP-PNP at 230C. J. Mol. Biol. 264:279-301.
17. Seymour, J., and D.J. DeRosier. 1987. The projection of a negatively-stained filamentous object down its central axis as revealed by image-reconstruction from tilt series. J. Microsc. (Oxf.). 148:195-210.
18. Steven, A.C., and M.A. Navia. 1982. Specificity of stain distribution in electron-micrographs of protein molecules contrasted with uranyl acetate. J. Microsc. (Oxf.). 128:145-155.
19. Unwin, P.N.T. 1974. Electron microscopy of the stacked disc aggregate of tobacco mosaic virus protein. Influence of electron irradiation on the stain distribution. J. Mol. Biol. 87:657-670.
20. Vibert, P.J. 1988. Domain structure of the myosin head in correlation-average images of shadowed molecules. J. Muscle Res. Cell Motil. 9:147-155.
21. Walker, M., and J. Trinick. 1986. Electron microscope study of the effect of temperature on the length of the tail of the myosin molecule. J. Mol. Biol. 192:661-667.
22. Walker, M., and J. Trinick. 1988. Visualization of domains in native and nucleotide-trapped myosin heads by negative staining. J. Muscle Res. Cell Motil. 9: 359-366.
23. Walker, M., P. Knight, and J. Trinick. 1985. Negative staining of myosin molecules. J. Mol. Biol. 184:535-542.
24. Whittaker, M., E.M. Wilson-Kubalek, J.E. Smith, L. Faust, R.A. Milligan, and H.L. Sweeney. 1995. A 35-Angstrom movement of smooth-muscle myosin on ADP release. Nature (Lond.). 378:748-751.