ArticleJournal of structural and functional genomics2010
Slow cooling and temperature-controlled protein crystallography.
Article in Journal of structural and functional genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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.
Who cites it
7 citing papers in PubMed.
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
- Solvent flows, conformation changes and lattice reordering in a cold protein crystal.Acta crystallographica. Section D, Structural biology · 2019Article
- Article
- Article
- Radiation decay of thaumatin crystals at three X-ray energies.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Global radiation damage: temperature dependence, time dependence and how to outrun it.Journal of synchrotron radiation · 2013Article
- Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites.Biochemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
In cryocrystallography, rapid sample cooling is generally deemed essential to prevent solvent crystallization and associated sample damage. We show that by carefully and completely removing all external solvent, many protein crystals can be successfully cooled to T = 100 K at only 0.1 K/s without additional penetrating cryoprotectants. Slow cooling provides an alternative when flash cooling fails, and enables diffraction studies of protein structure and function at all temperatures between T = 300 K and T = 100 K.
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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.