Evidence map›Paper›PMID 21964395›Full record

ReviewMethods (San Diego, Calif.)2011

A helical processing pipeline for EM structure determination of membrane proteins.

Lauren S Fisher, Andrew Ward, Ronald A Milligan, Nigel Unwin, Clinton S Potter, Bridget Carragher

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. The Electron Microscopy eXchange (EMX) initiative.Journal of structural biology · 2016
    Article
  2. Review
  3. 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

6 authors at 2 institutions in 2 countries.

Lauren S FisherThe National Resource for Automated Molecular Microscopy, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Andrew Ward
Ronald A Milligan
Nigel Unwin
Clinton S Potter
Bridget Carragher
Scripps Research Institute · USMRC Laboratory of Molecular Biology · GB

Funding

WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
Studies on Microtubule Binding ProteinsR37GM052468 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI MILLIGAN, RONALD A, WILSON-KUBALEK, ELIZABETH M · 2011 to 2020
$6.9M
STUDIES ON MICROTUBULE BINDING PROTEINSR01GM052468 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI MILLIGAN, RONALD A · 1995 to 2010
$5.0M
STRUCTURE DETERMINATION OF TUBULAR CRYSTALSR01GM061941 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI UNWIN, PETER NIGEL · 2000 to 2014
$2.9M
A Helical Crystallization Pipeline for Membrane Protein Structure by TEMR01GM095573 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2010 to 2013
$1.6M
ELECTRON MICROSCOPY OF MEMBRANE PROTEINS(RMI)R01GM075820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI MILLIGAN, RONALD A · 2005 to 2009
$1.6M
Medical Research Council MC_U105184294NCRR NIH HHS P41 RR017573NCRR NIH HHS RR017573NIGMS NIH HHS GM52468NIGMS NIH HHS GM61941NIGMS NIH HHS GM75820NIGMS NIH HHS R01 GM052468NIGMS NIH HHS R01 GM061941NIGMS NIH HHS R01 GM075820NIGMS NIH HHS R01 GM095573NIGMS NIH HHS R01GM095573NIGMS NIH HHS R37 GM052468
6 · The paper itself

Abstract

Electron crystallography plays a key role in the structural biology of integral membrane proteins (IMPs) by offering one of the most direct means of providing insight into the functional state of these molecular machines in their lipid-associated forms, and also has the potential to facilitate examination of physiologically relevant transitional states and complexes. Helical or tubular crystals, which are the natural product of proteins crystallizing on the surface of a cylindrical vesicle, offer some unique advantages, such as three-dimensional (3D) information from a single view, compared to other crystalline forms. While a number of software packages are available for processing images of helical crystals to produce 3D electron density maps, widespread exploitation of helical image reconstruction is limited by a lack of standardized approaches and the initial effort and specialized expertise required. Our goal is to develop an integrated pipeline to enable structure determination by transmission electron microscopy (TEM) of IMPs in the form of tubular crystals. We describe here the integration of standard Fourier-Bessel helical analysis techniques into Appion, an integrated, database-driven pipeline.

Indexed as

SoftwareATP-Binding Cassette TransportersBacterial ProteinsCrystallographyData Interpretation, StatisticalHumansMembrane ProteinsMicroscopy, Electron, TransmissionModels, MolecularProtein ConformationATP-Binding Cassette TransportersBacterial ProteinsMembrane ProteinsMsbA protein, Bacteria

Identifiers

PMID21964395
PMCPMC3262078
OpenAlexW1997380033

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.