Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G
Author:
Funder
National Science and Technology Council
Academia Sinica
Publisher
Elsevier BV
Subject
Structural Biology
Reference43 articles.
1. Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G;Tugarinov;J Mol Biol,2003
2. Anstrom DM, Kallio K, Remington SJ (2003) Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci 12:1822-1832. PMID: 12930982 {Medline}.
3. The product complex of M. tuberculosis malate synthase revisited;Anstrom;Protein Sci,2006
4. A simple method to predict protein flexibility using secondary chemical shifts;Berjanskii;J Am Chem Soc,2005
5. Casanal A, Lohkamp B, Emsley P (2020) Current developments in Coot for macromolecular model building of Electron Cryo-microscopy and Crystallographic Data. Protein Sci 29:1069-1078. PMID: 31730249 {Medline}.
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