Evidence map›Paper›PMID 37093476›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Effects of Ionic Liquids as Additives on Protein Crystallization.

Crissy L Tarver, Marc L Pusey

Abstract read
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Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Crissy L TarverDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Marc L PuseyDepartment of Chemistry, University of Alabama in Huntsville, Huntsville, AL, USA. mlp0041@uah.edu.

Funding

Macromolecule Crystallization Screening Results AnalysisR42GM116283 · NIGMS · IXPRESSGENES, INC. · PI PUSEY, MARC LEE · 2016 to 2017
$958k
NIGMS NIH HHS R42 GM116283
6 · The paper itself

Abstract

Protein crystallization is a complex process, where every component and physical parameter of the crystallization process may have an effect on the outcome. Crystallization conditions are typically arrived at by a screening process, where the target is subjected to a broad array of solution conditions with the goal of obtaining at least one condition that can be carried on to a structure. Ionic liquids (IL) have been found to be useful additives for improving the outcomes of the crystallization process, with existing data indicating that the IL structure has an effect. We describe a method for quickly preparing a series of solutions that vary in just one component, in this case a series of ILs that are used as crystallization additives. The method results in a screening grid, where the crystallization conditions being tested are constant in any one column in the Y dimension and they ILs are constant in any one row in the X dimension. This provides a systematic approach to determining effective ILs for obtaining crystals from a limited set of promising starting crystallization conditions. The approach generates an X-Y array of conditions, where the basic precipitant conditions are kept constant in one plate dimension and the additives are kept constant in the second dimension, generating a 12 × 8 array of conditions. This approach would also be useful for surveying other classes of protein crystallization additives in a systematic fashion.

Indexed as

Ionic LiquidsCrystallizationProteinsIonic LiquidsProteinsAdditivesCrystallization screeningIonic liquidsProtein crystallization

Identifiers

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Registered trials

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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.