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

Chari, A., Haselbach, D., Kirves, J. M., Ohmer, J., Paknia, E., Fischer, N., et al. (2015). ProteoPlex: Stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nature Methods, 12(9), 859-865. doi:10.1038/NMETH.3493.

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 Creators:
Chari, A.1, Author           
Haselbach, D.2, Author           
Kirves, J. M.2, Author           
Ohmer, J., Author
Paknia, E., Author
Fischer, N.2, Author           
Ganichkin, O.3, Author           
Moller, V., Author
Frye, J. J., Author
Petzold, G., Author
Jarvis, M., Author
Tietzel, M., Author
Grimm, C., Author
Peters, J. M., Author
Schulman, B. A., Author
Tittmann, K., Author
Markl, J., Author
Fischer, U., Author
Stark, H.2, Author           
Affiliations:
1Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society, ou_3265855              
2Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society, ou_578577              
3Research Group of X-Ray Crystallography, MPI for biophysical chemistry, Max Planck Society, ou_578578              

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 Abstract: Molecular machines or macromolecular complexes are supramolecular assemblies of biomolecules with a variety of functions. Structure determination of these complexes in a purified state is often tedious owing to their compositional complexity and the associated relative structural instability. To improve the stability of macromolecular complexes in vitro, we present a generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behavior in the presence of various buffers and small molecules. The method includes the automated analysis of thermal unfolding curves based on a biophysical unfolding model for complexes. We found that under stabilizing conditions, even large multicomponent complexes reveal an almost ideal two-state unfolding behavior. We envisage an improved biochemical understanding of purified macromolecules as well as a substantial boost in successful macromolecular complex structure determination by both X-ray crystallography and cryo-electron microscopy.

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Language(s): eng - English
 Dates: 2015-08-032015-09
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/NMETH.3493
 Degree: -

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Title: Nature Methods
Source Genre: Journal
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Pages: - Volume / Issue: 12 (9) Sequence Number: - Start / End Page: 859 - 865 Identifier: -