Literature DB >> 8727314

Why are protein crystallographic R-values so high?

E E Lattman.   

Abstract

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Year:  1996        PMID： 8727314     DOI： 10.1002/prot.340250102

Source DB:  PubMed          Journal:  Proteins        ISSN： 0887-3585


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  4 in total

1.  Systematic analysis of residual density suggests that a major limitation in well-refined X-ray structures of proteins is the omission of ordered solvent.

Authors:  Jimin Wang
Journal:  Protein Sci       Date:  2017-03-07       Impact factor: 6.725

2.  X-ray radiation-induced addition of oxygen atoms to protein residues.

Authors:  Jimin Wang
Journal:  Protein Sci       Date:  2016-07-08       Impact factor: 6.725

3.  Interpretation of ensembles created by multiple iterative rebuilding of macromolecular models.

Authors:  Thomas C Terwilliger; Ralf W Grosse-Kunstleve; Pavel V Afonine; Paul D Adams; Nigel W Moriarty; Peter Zwart; Randy J Read; Dusan Turk; Li Wei Hung
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2007-04-21

4.  Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: the dual role of deposited experimental data.

Authors:  Thomas C Terwilliger; Gerard Bricogne
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2014-09-30
  4 in total

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