Evidence map›Paper›PMID 20713010›Full record

ArticleBiophysical journal2010

In situ muGISAXS: I. Experimental setup for submicron study of protein nucleation and growth.

Ronald Gebhardt, Eugenia Pechkova, Christian Riekel, Claudio Nicolini

Erratum issuedAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors.

Ronald GebhardtNanoworld Institute, CIRSDNNOB-University of Genoa, Genoa, Italy.
Eugenia Pechkova
Christian Riekel
Claudio Nicolini

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we used microbeam grazing-incidence small-angle x-ray scattering (muGISAXS) to investigate in situ protein nucleation and crystal growth assisted by a protein nanotemplate, and introduced certain innovations to improve the method. Our aim was to understand the protein nanotemplate method in detail, as this method has been shown to be capable of accelerating and increasing crystal size and quality, as well as inducing crystallization of proteins that are not crystallizable by classical methods. The nanotemplate experimental setup was used for drops containing growing protein crystals at different stages of nucleation and growth. Two model proteins, lysozyme and thaumatin, were used under unique flow conditions to differentially probe protein crystal nucleation and growth.

Indexed as

Particle SizeScattering, Small AngleAnimalsChickensCrystallizationModels, MolecularMuramidaseNanostructuresPlant ProteinsX-Ray DiffractionMuramidasePlant Proteinsthaumatin protein, plant

Identifiers

PMID20713010
PMCPMC2920631

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.