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citation_title: ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space
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keywords: Protein folding, Molecular biophysics, X-ray crystallography, Cryoelectron microscopy
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citation_publisher: Nature Publishing Group
citation_journal_title: Nature Methods
description: 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.
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citation_date: 2015-09-01
title: Evaluation of the quality of ProteoPlex data approximation. : ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space : Nature Methods : Nature Publishing Group
DC.title: ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space
DC.date: 2015-08-03
prism.issn: 1548-7091
DC.publisher: Nature Publishing Group
citation_online_date: 2015-08-03
WT.cg_n: Nature Methods
DC.creator: Ashwin Chari
prism.issue: 9
DC.identifier: doi:10.1038/nmeth.3493
dc:title: Evaluation of the quality of ProteoPlex data approximation. : ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space : Nature Methods : Nature Publishing Group
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prism.publicationDate: 2015-08-03
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DC.rights: © 2015 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
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citation_author: Ashwin Chari
citation_issue: 9
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prism.volume: 12
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prism.publicationName: Nature Methods
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WT.site_id_name: Max Planck Inst for Biophysical Chemistry (Karl Friedrich Bonhoeffer Inst)
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prism.copyright: © 2015 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.