Evidence map›Paper›PMID 21311730›Full record

ArticleSoft matter2009

An ion-channel-containing model membrane: structural determination by magnetic contrast neutron reflectometry.

Stephen A Holt, Anton P Le Brun, Charles F Majkrzak, Duncan J McGillivray, Frank Heinrich, Mathias Lösche, Jeremy H Lakey

Abstract read
In one paragraph

Article in Soft matter, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Twin-compartment solid-liquid cells for neutron reflectometry.Journal of applied crystallography · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Using refnx to Model Neutron Reflectometry Data from Phospholipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. An Accurate In Vitro Model of theAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2015
    Article
  19. An accurate in vitro model of the E. coli envelope.Angewandte Chemie (International ed. in English) · 2015
    Article
  20. Article
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

7 authors.

Stephen A HoltISIS, Rutherford Appleton Laboratory, Science and Technology Facilities Council, Didcot, OX11 0QX, UK.
Anton P Le Brun
Charles F Majkrzak
Duncan J McGillivray
Frank Heinrich
Mathias Lösche
Jeremy H Lakey

Funding

STRUCTURAL&FUNCTIONAL INESTIGATIONS OF AB OLIGOMER INTERACTION/SYNTHETIC MEMBRANEP01AG032131 · NIA · CARNEGIE-MELLON UNIVERSITY · PI DESEMO, MARKUS · 2009 to 2011
$1.9M
NIA NIH HHS P01 AG032131
6 · The paper itself

Abstract

To many biophysical characterisation techniques, biological membranes appear as two-dimensional structures with details of their third dimension hidden within a 5 nm profile. Probing this structure requires methods able to discriminate multiple layers a few Ångströms thick. Given sufficient resolution, neutron methods can provide the required discrimination between different biochemical components, especially when selective deuteration is employed. We have used state-of-the-art neutron reflection methods, with resolution enhancement via magnetic contrast variation to study an oriented model membrane system. The model is based on the Escherichia coli outer membrane protein OmpF fixed to a gold surface via an engineered cysteine residue. Below the gold is buried a magnetic metal layer which, in a magnetic field, displays different scattering strengths to spin-up and spin-down neutrons. This provides two independent datasets from a single biological sample. Simultaneous fitting of the two datasets significantly refines the resulting model. A β-mercaptoethanol (βME) passivating surface, applied to the gold to prevent protein denaturation, is resolved for the first time as an 8.2 ± 0.6 Å thick layer, demonstrating the improved resolution and confirming that this layer remains after OmpF assembly. The thiolipid monolayer (35.3 ± 0.5 Å), assembled around the OmpF is determined and finally a fluid DMPC layer is added (total lipid thickness 58.7 ± 0.9 Å). The dimensions of trimeric OmpF in isolation (53.6 ± 2.5 Å), after assembly of lipid monolayer (57.5 ± 0.9 Å) and lipid bilayer (58.7 ± 0.9 Å), are precisely determined and show little variation.

Identifiers

PMID21311730
PMCPMC3035324

What OpenQuestion holds

Textmetadata
LicenceTDM
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.