Evidence map›Paper›PMID 19554626›Full record

ArticleProtein science : a publication of the Protein Society2009

Determination and application of empirically derived detergent phase boundaries to effectively crystallize membrane proteins.

Mary Koszelak-Rosenblum, Adam Krol, Namrita Mozumdar, Kristin Wunsch, Adam Ferin, Eleanor Cook, Christina K Veatch, Raymond Nagel, Joseph R Luft, George T Detitta and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Crystal structure of rofecoxib bound to human cyclooxygenase-2.Acta crystallographica. Section F, Structural biology communications · 2016
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  16. Review
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  18. Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening.Acta crystallographica. Section D, Biological crystallography · 2011
    Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Mary Koszelak-RosenblumHauptman-Woodward Medical Research Institute, Buffalo, New York 14203.
Adam Krol
Namrita Mozumdar
Kristin Wunsch
Adam Ferin
Eleanor Cook
Christina K Veatch
Raymond Nagel
Joseph R Luft
George T Detitta
Michael G Malkowski
Hauptman-Woodward Medical Research Institute · USUniversity at Buffalo, State University of New York · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
TOOLS FOR HIGH THROUGHPUT STRUCTURAL BIOLOGYU54GM074899 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI DETITTA, GEORGE T · 2005 to 2010
$16.5M
NCRR NIH HHS P41 RR001646NIGMS NIH HHS DMR-0225180NIGMS NIH HHS U54 GM074899
6 · The paper itself

Abstract

Elucidating the structures of membrane proteins is essential to our understanding of disease states and a critical component in the rational design of drugs. Structural characterization of a membrane protein begins with its detergent solubilization from the lipid bilayer and its purification within a functionally stable protein-detergent complex (PDC). Crystallization of the PDC typically occurs by changing the solution environment to decrease solubility and promote interactions between exposed hydrophilic surface residues. As membrane proteins have been observed to form crystals close to the phase separation boundaries of the detergent used to form the PDC, knowledge of these boundaries under different chemical conditions provides a foundation to rationally design crystallization screens. We have carried out dye-based detergent phase partitioning studies using different combinations of 10 polyethylene glycols (PEG), 11 salts, and 11 detergents to generate a significant amount of chemically diverse phase boundary data. The resulting curves were used to guide the formulation of a 1536-cocktail crystallization screen for membrane proteins. We are making both the experimentally derived phase boundary data and the 1536 membrane screen available through the high-throughput crystallization facility located at the Hauptman-Woodward Institute. The phase boundary data have been packaged into an interactive Excel spreadsheet that allows investigators to formulate grid screens near a given phase boundary for a particular detergent. The 1536 membrane screen has been applied to 12 membrane proteins of unknown structures supplied by the structural genomics and structural biology communities, with crystallization leads for 10/12 samples and verification of one crystal using X-ray diffraction.

Indexed as

AnimalsCrystallizationDetergentsMembrane ProteinsPolyethylene GlycolsDetergentsMembrane ProteinsPolyethylene Glycols

Identifiers

PMID19554626
PMCPMC2777358
OpenAlexW2075930146

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.