Evidence map›Paper›PMID 33559608›Full record

ArticleActa crystallographica. Section D, Structural biology2021

Homogeneous batch micro-crystallization of proteins from ammonium sulfate.

Claudia Stohrer, Sam Horrell, Susanne Meier, Marta Sans, David von Stetten, Michael Hough, Adrian Goldman, Diana C F Monteiro, Arwen R Pearson

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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  10. Best practices for time-resolved serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2022
    Review
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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

9 authors at 5 institutions in 4 countries.

Claudia StohrerBiomedical Sciences, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom.ORCID 0000-0001-9053-7722
Sam HorrellHamburg Centre for Ultrafast Imaging, Institute for Nanostructure and Solid State Physics, Universität Hamburg, CFEL, Building 99, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0001-6355-8640
Susanne MeierHamburg Centre for Ultrafast Imaging, Institute for Nanostructure and Solid State Physics, Universität Hamburg, CFEL, Building 99, Luruper Chaussee 149, 22761 Hamburg, Germany.
Marta SansHamburg Centre for Ultrafast Imaging, Institute for Nanostructure and Solid State Physics, Universität Hamburg, CFEL, Building 99, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0002-0102-8190
David von StettenEuropean Molecular Biology Laboratory (EMBL), Hamburg Unit c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany.ORCID 0000-0001-7906-9788
Michael HoughSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom.ORCID 0000-0001-7377-6713
Adrian GoldmanBiomedical Sciences, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, United Kingdom.ORCID 0000-0001-8032-9700
Diana C F MonteiroHamburg Centre for Ultrafast Imaging, Institute for Nanostructure and Solid State Physics, Universität Hamburg, CFEL, Building 99, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0002-6318-7306
Arwen R PearsonHamburg Centre for Ultrafast Imaging, Institute for Nanostructure and Solid State Physics, Universität Hamburg, CFEL, Building 99, Luruper Chaussee 149, 22761 Hamburg, Germany.ORCID 0000-0001-8499-7490
Universität Hamburg · DEUniversity of Leeds · GBEuropean Molecular Biology Laboratory · DEHauptman-Woodward Medical Research Institute · USUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M022714/1Bundesministerium für Bildung, Wissenschaft und Forschung 05K16GU1Federal Excellence Cluster Hamburg Centre for Ultrafast Imaging EXC 1074H2020 Marie Skłodowska-Curie Actions 722687
6 · The paper itself

Abstract

The emergence of X-ray free-electron lasers has led to the development of serial macromolecular crystallography techniques, making it possible to study smaller and more challenging crystal systems and to perform time-resolved studies on fast time scales. For most of these studies the desired crystal size is limited to a few micrometres, and the generation of large amounts of nanocrystals or microcrystals of defined size has become a bottleneck for the wider implementation of these techniques. Despite this, methods to reliably generate microcrystals and fine-tune their size have been poorly explored. Working with three different enzymes, L-aspartate α-decarboxylase, copper nitrite reductase and copper amine oxidase, the precipitating properties of ammonium sulfate were exploited to quickly transition from known vapour-diffusion conditions to reproducible, large-scale batch crystallization, circumventing the tedious determination of phase diagrams. Furthermore, the specific ammonium sulfate concentration was used to fine-tune the crystal size and size distribution. Ammonium sulfate is a common precipitant in protein crystallography, making these findings applicable to many crystallization systems to facilitate the production of large amounts of microcrystals for serial macromolecular crystallography experiments.

Indexed as

Ammonium SulfateCrystallography, X-RayMacromolecular SubstancesProteinsAmmonium SulfateMacromolecular SubstancesProteinsammonium sulfatebatch crystallizationmicrocrystalsserial crystallography

Identifiers

PMID33559608
PMCPMC7869895
OpenAlexW3122159819

What OpenQuestion holds

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LicenceCC BY
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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.