Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein–nucleic acid complex crystals

By K. Kantardjieff, B. Rupp. 2003

744 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

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Citations in the corpus

Using SAD data in Phaser (2011, neutral): “The structure can be solved by molecular replacement using goat -lactalbumin (PDB code 1fkq; Horii et al., 2001), a relatively poor model that shares 45% sequence identity.”
Automated search-model discovery and preparation for structure solution by molecular replacement. (2007, positive): “The latter is based on the Matthews coefficient probabilities proposed recently by Kantardjieff & Rupp (2003).”
Can I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal (2016, background): “The solvent content for many macromolecular crystals is near 50%, although occasionally it may be much higher or lower (Matthews, 1968; Kantardjieff & Rupp, 2003; Weichenberger & Rupp, 2014).”
On the use of logarithmic scales for analysis of diffraction data (2009, methodology): “This agrees with the previous demonstration by Kantardjieff & Rupp (2003) 1286 Urzhumtsev et al. Logarithmic scales in diffraction data analysis Acta Cryst.”
Web-based visualisation and analysis of 3D electron-microscopy data from EMDB and PDB (2013, background): “the mass density of macromolecular complexes varies considerably (Kantardjieff and Rupp, 2003), with estimates ranging from 1.”
Decision making in xia2 (2013, methodology): “If a sequence file is found alongside the diffraction data or is provided in the input file, an estimate of the number of molecules in the asymmetric unit is made following a probabilistic procedure (Kantardjieff & Rupp, 2003) and an appropriate solvent content is provided to the TRUNCATE procedure.”
Structure and ligand binding of the glutamine-II riboswitch (2019, background): “From crystal density considerations (19,20), two RNA molecules were expected to be present in the asymmetric unit.”
Computational design of a protein crystal (2012, background): “The solvent content (36%) is less than that observed for typical protein crystals (51%), hexagonal protein crystals (57%), and protein crystals with four polypeptide chains in the asymmetric unit (51%) (21, 55, 56).”