Evidence map›Paper›PMID 20196072›Full record

ReviewProtein science : a publication of the Protein Society2010

A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.

Andrea F Moon, Geoffrey A Mueller, Xuejun Zhong, Lars C Pedersen

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

99 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
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  3. Crystal Structure and Catalytic Mechanism of the cis-Eunicellane Cyclase AriE.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
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  8. RNA-Binding Protein-Mediated mRNA Deadenylation in Mammalian Cell Extracts.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  13. Review
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  16. Structure of the RECK CC domain, an evolutionary anomaly.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
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  19. Article
  20. Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020
    Review

39 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Andrea F MoonLaboratory of Structural Biology, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709, USA.
Geoffrey A Mueller
Xuejun Zhong
Lars C Pedersen
National Institute of Environmental Health Sciences · US

Funding

Structural and Functional Characterization of AllergensZIAES102906 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MUELLER, GEOFFREY · 2010 to 2025
$10.0M
Crystallographic studies of macromolecular structuresZIAES102645 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI PEDERSEN, LARS · 2009 to 2017
$9.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Protein crystallographers are often confronted with recalcitrant proteins not readily crystallizable, or which crystallize in problematic forms. A variety of techniques have been used to surmount such obstacles: crystallization using carrier proteins or antibody complexes, chemical modification, surface entropy reduction, proteolytic digestion, and additive screening. Here we present a synergistic approach for successful crystallization of proteins that do not form diffraction quality crystals using conventional methods. This approach combines favorable aspects of carrier-driven crystallization with surface entropy reduction. We have generated a series of maltose binding protein (MBP) fusion constructs containing different surface mutations designed to reduce surface entropy and encourage crystal lattice formation. The MBP advantageously increases protein expression and solubility, and provides a streamlined purification protocol. Using this technique, we have successfully solved the structures of three unrelated proteins that were previously unattainable. This crystallization technique represents a valuable rescue strategy for protein structure solution when conventional methods fail.

Indexed as

Amino Acid SequenceAnimalsAntigens, DermatophagoidesArabidopsisArabidopsis ProteinsArthropod ProteinsBase SequenceChickensCrystallizationCrystallography, X-RayDermatophagoides pteronyssinusEntropyMaltose-Binding ProteinsModels, MolecularMolecular Sequence DataPeriplasmic Binding ProteinsAntigens, DermatophagoidesArabidopsis ProteinsArthropod ProteinsDermatophagoides pteronyssinus antigen p 7Maltose-Binding ProteinsPeriplasmic Binding ProteinsRACK1 protein, ArabidopsisReceptors, Cell SurfaceReceptors for Activated C KinaseRecombinant Fusion ProteinsSulfotransferases

Identifiers

PMID20196072
PMCPMC2868234
OpenAlexW2164350157

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.