Do we see what we should see? Describing non-covalent interactions in protein structures including precision.

ABSTRACT: The power of X-ray crystal structure analysis as a technique is to 'see where the atoms are'. The results are extensively used by a wide variety of research communities. However, this 'seeing where the atoms are' can give a false sense of security unless the precision of the placement of the atoms has been taken into account. Indeed, the presentation of bond distances and angles to a false precision (i.e. to too many decimal places) is commonplace. This article has three themes. Firstly, a basis for a proper representation of protein crystal structure results is detailed and demonstrated with respect to analyses of Protein Data Bank entries. The basis for establishing the precision of placement of each atom in a protein crystal structure is non-trivial. Secondly, a knowledge base harnessin

SUBMITTER: Gurusaran M 

PROVIDER: S-EPMC4104967 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature