Myosin motors walk the walk

Science

Volumn 300, Issue 5628, 2003, Pages 2045-2046

  Molloy, Justin E ^a   Veigel, Claudia ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MYOSIN V; ACTIN; FLUORESCENT DYE; MOLECULAR MOTOR; MYOSIN LIGHT CHAIN;

BIOLOGY;

ACTIN FILAMENT; FLUORESCENCE MICROSCOPY; HYDROLYSIS; MODEL; MOVEMENT (PHYSIOLOGY); MUSCLE CONTRACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; REVIEW; BINDING SITE; BIOLOGICAL MODEL; CHEMISTRY; KINETICS; METABOLISM; MICROFILAMENT; NOTE; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

ACTINS; ADENOSINE TRIPHOSPHATE; BINDING SITES; FLUORESCENT DYES; HYDROLYSIS; KINETICS; MICROFILAMENTS; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; MOLECULAR MOTOR PROTEINS; MYOSIN LIGHT CHAINS; MYOSIN TYPE V; PROTEIN STRUCTURE, TERTIARY;

EID: 0037804221     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1087148     Document Type: Review

References (18)

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18. Such experiments require that the mechanical stability of the microscope is in the nanometer range and that the camera system noise (dark counts and readout noise) is trivial compared to the photon counting noise. Accuracy in determining the centroid of a diffraction-limited spot is then simply a matter of counting statistics: The standard error in estimating the mean position is related to the spot size (about 150-nm radius at half height) and the square root of the number of photons collected (14,000 per half-second bin). Yildiz et al. had a resolution of about 1.5 nm.