ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space

ProteoPlex optimizes buffer conditions for the isolation and purification of macromolecular complexes. The concurrent complex stabilization is beneficial for structure determination using X-ray crystallography or cryo-electron microscopy. Molecular machines or macromolecular complexes are supramolec...

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Veröffentlicht in:	Nature methods 2015-09, Vol.12 (9), p.859-865
Hauptverfasser:	Chari, Ashwin, Haselbach, David, Kirves, Jan-Martin, Ohmer, Juergen, Paknia, Elham, Fischer, Niels, Ganichkin, Oleg, Möller, Vanessa, Frye, Jeremiah J, Petzold, Georg, Jarvis, Marc, Tietzel, Michael, Grimm, Clemens, Peters, Jan-Michael, Schulman, Brenda A, Tittmann, Kai, Markl, Jürgen, Fischer, Utz, Stark, Holger
Format:	Artikel
Sprache:	eng
Schlagworte:	14/28 14/34 631/1647/2258/1258/1259 631/1647/2258/1266 631/45/470 631/57/2272 82/83 Algorithms Binding Sites Bioinformatics Biological Microscopy Biological Techniques Biomedical Engineering/Biotechnology Biomolecules Buffers Computer Simulation Crystallization Crystallography Electron microscopy Homogeneity Life Sciences Matrix Medical research Medicine, Experimental Methods Models, Chemical Models, Molecular Molecular biology Molecular machines Multiprotein Complexes - chemistry Multiprotein Complexes - ultrastructure Protein Binding Protein Conformation Protein Folding Proteomics Software Solubility X-ray crystallography
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