The benefits of atomic resolution.
By Z. Dauter, V. Lamzin, Keith S. Wilson. 1997
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Pavel V. Afonine
- Paul D. Adams
- Nigel W. Moriarty
- T. C. Terwilliger
- D. Liebschner
- Nathaniel Echols
- J. Headd
- R. Grosse-Kunstleve
Citations in the corpus
- 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.”
- Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms. (1999, background): “These analyses emphasize the truly revolutionary accuracy and detail attainable in the new wave of protein crystallographic structures at atomic resolution (Dauter et al., 1997).”
- Structure quality and target parameters (2006, background): “There are now two sources of structural information of sufficient quality for use as restraints in structure refinement: chemical fragments from the Cambridge Structural Database (CSD) and the very high resolution protein structures that can be refined without recourse to restraining parameters (Lon”