Localization atomic force microscopy

• Published in: Nature (London) Vol. 594; no. 7863; pp. 385 - 390
• Main Authors: Heath, George R., Kots, Ekaterina, Robertson, Janice L., Lansky, Shifra, Khelashvili, George, Weinstein, Harel, Scheuring, Simon
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 17.06.2021; Nature Publishing Group
• Subjects: 631/1647/2204/1262; 631/57/2265; 631/57/2282; 639/766/930/328/1262; 639/925/930/2735; Algorithms; Ambient temperature; Amino acids; Amino Acids - chemistry; Annexin A5 - chemistry; Annexin A5 - ultrastructure; Aquaporins - chemistry; Aquaporins - ultrastructure; Atomic force microscopy; Biomolecules; Chloride Channels - chemistry; Chloride Channels - ultrastructure; Datasets as Topic; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - ultrastructure; Humanities and Social Sciences; Humans; Hydrogen-Ion Concentration; Image acquisition; Image processing; Image reconstruction; Image resolution; Localization; Methods; Microscopy; Microscopy, Atomic Force - methods; Microscopy, Atomic Force - standards; Molecular Dynamics Simulation; Molecular modelling; multidisciplinary; Noise; Physiology; Proteins; Science; Science (multidisciplinary); Simulation; Structural analysis; Structure; Topography; United States

Understanding structural dynamics of biomolecules at the single-molecule level is vital to advancing our knowledge of molecular mechanisms. Currently, there are few techniques that can capture dynamics at the sub-nanometre scale and in physiologically relevant conditions. Atomic force microscopy (AF...