title: Structure of the globular protein vicilin revealed by scanning tunnelling microscopy.
abstract: Scanning tunnelling microscopy (s.t.m.) has been used to study the structure of the non-crystalline globular protein vicilin. Molecules were deposited on amorphous carbon substrates and imaged both in air and in vacuo without additional sample preparation. Current-voltage plots of an individual protein molecule are also reported. The s.t.m. images are compared with conventional transmission electron micrographs and with a model of vicilin based on small-angle synchrotron X-ray scattering data.
authors.affiliation: Department of Engineering, Cambridge, UK.
authors.forename: M E
authors.initials: ME
authors.lastname: Welland
authors.forename: M J
authors.initials: MJ
authors.lastname: Miles
authors.forename: N
authors.initials: N
authors.lastname: Lambert
authors.forename: V J
authors.initials: VJ
authors.lastname: Morris
authors.forename: J H
authors.initials: JH
authors.lastname: Coombs
authors.forename: J B
authors.initials: JB
authors.lastname: Pethica
mesh_terms: D004553:Electric Conductivity; D008854:Microscopy, Electron; D016252:Microscopy, Scanning Tunneling; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000648:ultrastructure*; D055314:Seed Storage Proteins; D014961:X-Ray Diffraction
chemical_list: D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C015575:vicilin protein, plant