A Protein Structure is Only as Good as the Data

  • Benno P. Schoenborn
Chapter
Part of the Basic Life Sciences book series (BLSC, volume 27)

Abstract

In the interpretation of any protein structure derived from diffraction data, one has to try to assess the reliability of the derived atomic positions and atomic species. In the neutron case, it is possible to localize hydrogen atoms (1). This, however, just about doubles the total number of atoms to be derived with about the same number of reflections. In addition, neutron data are often of poorer statistical quality than their x-ray counterparts because of low source flux and the very high background caused by the incoherent scattering of hydrogen atoms. Thus in neutron protein crystallography there is a higher uncertainty in the measured structure factor, in addition to uncertainties in phasing and refinement.

Keywords

Reciprocal Lattice Beam Divergence Detector Resolution Crystal Rotation Crystal Mosaic 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Benno P. Schoenborn
    • 1
  1. 1.Biology DepartmentBrookhaven National LaboratoryUptonUSA

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