---
res:
  bibo_abstract:
  - Cryo-electron tomography combined with image processing by sub-tomogram averaging
    is unique in its power to resolve the structures of proteins and macromolecular
    complexes in situ. Limitations of the method, including the low signal to noise
    ratio within individual images from cryo-tomographic datasets and difficulties
    in determining the defocus at which the data was collected, mean that to date
    the very best structures obtained by sub-tomogram averaging are limited to a resolution
    of approximately 15. Å. Here, by optimizing data collection and defocus determination
    steps, we have determined the structure of assembled Mason-Pfizer monkey virus
    Gag protein using sub-tomogram averaging to a resolution of 8.5. Å. At this resolution
    alpha-helices can be directly and clearly visualized. These data demonstrate for
    the first time that high-resolution structural information can be obtained from
    cryo-electron tomograms using sub-tomogram averaging. Sub-tomogram averaging has
    the potential to allow detailed studies of unsolved and biologically relevant
    structures under biologically relevant conditions.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Florian
      foaf_name: Florian Schur
      foaf_surname: Schur
      foaf_workInfoHomepage: http://www.librecat.org/personId=48AD8942-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0003-4790-8078
  - foaf_Person:
      foaf_givenName: Wim
      foaf_name: Hagen, Wim J
      foaf_surname: Hagen
  - foaf_Person:
      foaf_givenName: Alex
      foaf_name: De Marco, Alex
      foaf_surname: De Marco
  - foaf_Person:
      foaf_givenName: John
      foaf_name: Briggs, John A
      foaf_surname: Briggs
  bibo_doi: 10.1016/j.jsb.2013.10.015
  bibo_issue: '3'
  bibo_volume: 184
  dct_date: 2013^xs_gYear
  dct_publisher: Academic Press@
  dct_title: Determination of protein structure at 8.5Å resolution using cryo-electron
    tomography and sub-tomogram averaging@
...