Protein crystallography at subatomic resolution

By T. Petrova, A. Podjarny. 2004

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Towards automated crystallographic structure refinement with phenix.refine (2012, background): “In addition, when refining a structure at such a high resolution one usually looks for very fine structural details (for example, Dauter et al., 1995, 1997; Vrielink & Sampson, 2003; Petrova & Podjarny, 2004), which are often only seen as subtle features in residual maps close to the noise level.”
Joint X-ray and neutron refinement with phenix.refine. (2010, background): “Only subatomic resolution1 structures, of which there are currently only 358 out of a total of over 58 750 PDB entries (Bernstein et al., 1977; Berman et al., 2000), reliably reveal the position of some H atoms in residual maps (see, for example, Petrova & Podjarny, 2004; Ahmed et al., 2007).”
Biological Crystallography Structure of Acostatin, a Dimeric Disintegrin from Southern Copperhead (agkistrodon Contortrix Contortrix), at 1.7 a ˚ Resolution (background): “The new information obtained from such macromolecular studies has been discussed in a number of articles (see for example reviews Dauter et al., 1995, 1997; Vrielenk & Sampson, 2003; Petrova & Podjarny, 2004, and numerous references therein).”