Evidence map›Paper›PMID 10975577›Full record

ArticleProtein science : a publication of the Protein Society2000

Static light scattering studies of OmpF porin: implications for integral membrane protein crystallization.

C Hitscherich, J Kaplan, M Allaman, J Wiencek, P J Loll

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

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0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026
    Review
  2. Article
  3. Review
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  7. Applications of the second virial coefficient: protein crystallization and solubility. Corrigendum.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  8. Article
  9. Membrane proteins, detergents and crystals: what is the state of the art?Acta crystallographica. Section F, Structural biology communications · 2014
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. When worlds colloid.Protein science : a publication of the Protein Society · 2006
    Article
  15. Article
  16. Article
  17. 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

5 authors.

C HitscherichDepartment of Chemical and Biochemical Engineering, University of Iowa, Iowa City 52242, USA.
J Kaplan
M Allaman
J Wiencek
P J Loll

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integral membrane proteins carry out some of the most important functions of living cells, yet relatively few details are known about their structures. This is due, in large part, to the difficulties associated with preparing membrane protein crystals suitable for X-ray diffraction analysis. Mechanistic studies of membrane protein crystallization may provide insights that will aid in determining future membrane protein structures. Accordingly, the solution behavior of the bacterial outer membrane protein OmpF porin was studied by static light scattering under conditions favorable for crystal growth. The second osmotic virial coefficient (B22) was found to be a predictor of the crystallization behavior of porin, as has previously been found for soluble proteins. Both tetragonal and trigonal porin crystals were found to form only within a narrow window of B22 values located at approximately -0.5 to -2 X 10(-4) mol mL g(-2), which is similar to the "crystallization slot" observed for soluble proteins. The B22 behavior of protein-free detergent micelles proved very similar to that of porin-detergent complexes, suggesting that the detergent's contribution dominates the behavior of protein-detergent complexes under crystallizing conditions. This observation implies that, for any given detergent, it may be possible to construct membrane protein crystallization screens of general utility by manipulating the solution properties so as to drive detergent B22 values into the crystallization slot. Such screens would limit the screening effort to the detergent systems most likely to yield crystals, thereby minimizing protein requirements and improving productivity.

Indexed as

Bacterial Outer Membrane ProteinsCrystallizationCrystallographyDetergentsDialysisEscherichia coliLightMicellesModels, MolecularPolyethylene GlycolsPorinsProtein ConformationScattering, RadiationSoftwareX-Ray DiffractionBacterial Outer Membrane ProteinsDetergentsMicellesOmpF proteinPolyethylene GlycolsPorins

Identifiers

PMID10975577
PMCPMC2144733

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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.