ArticleCrystal growth & design2011
Developing a Fluorescence-based Approach to Screening for Macromolecule Crystallization Conditions.
Article in Crystal growth & design, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Interrogating Detergent Desolvation of Nanopore-Forming Proteins by Fluorescence Polarization Spectroscopy.Analytical chemistry · 2017Article
- A crystallization apparatus for temperature-controlled flow-cell dialysis with real-time visualization.Journal of applied crystallography · 2016Article
- Microseed matrix screening for optimization in protein crystallization: what have we learned?Acta crystallographica. Section F, Structural biology communications · 2014Article
- Introduction to protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2014Review
- Some practical guidelines for UV imaging in the protein crystallization laboratory.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Current macromolecule crystallization screening methods rely on the random testing of crystallization conditions, in the hope that one or more will yield positive results, crystals. Most plate outcomes are either clear or precipitated solutions, which results are routinely discarded by the experimenter. However, many of these may in fact be close to crystallization conditions, which fact is obscured by the nature of the apparent outcome. We are developing a fluorescence-based approach to the determination of crystallization conditions, which approach can also be used to assess conditions that may be close to those that would give crystals. The method uses measurements of fluorescence anisotropy and intensity. The method was first tested using model proteins, with likely outcomes as determined by fluorescence measurements where the plate data showed either clear or precipitated solutions being subjected to optimization screening. The results showed a ~83% increase in the number of crystallization conditions. The method was then tried as the sole screening method with a number of test proteins. In every case at least one or more crystallization conditions were found, and it is estimated that ~53% of these would not have been found using a plate screen.
Identifiers
What OpenQuestion holds
Registered trials
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.