ArticleActa crystallographica. Section D, Structural biology2016
Thermal contraction of aqueous glycerol and ethylene glycol solutions for optimized protein-crystal cryoprotection.
Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- DSC Study of Conjugated Recombinant Antigen Solution.ACS omega · 2026Article
- Interplay of vitrification and ice formation in a cryoprotectant aqueous solution at low temperature.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Solvent flows, conformation changes and lattice reordering in a cold protein crystal.Acta crystallographica. Section D, Structural biology · 2019Article
- Article
- The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.Acta crystallographica. Section D, Structural biology · 2018Article
- Density and electron density of aqueous cryoprotectant solutions at cryogenic temperatures for optimized cryoprotection and diffraction contrast.Acta crystallographica. Section D, Structural biology · 2018Article
- Measuring the Densities of Aqueous Glasses at Cryogenic Temperatures.Journal of visualized experiments : JoVE · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The thermal contraction of aqueous cryoprotectant solutions on cooling to cryogenic temperatures is of practical importance in protein cryocrystallography and in biological cryopreservation. In the former case, differential contraction on cooling of protein molecules and their lattice relative to that of the internal and surrounding solvent may lead to crystal damage and the degradation of crystal diffraction properties. Here, the amorphous phase densities of aqueous solutions of glycerol and ethylene glycol at T = 77 K have been determined. Densities with accuracies of <0.5% to concentrations as low as 30%(w/v) were determined by rapidly cooling drops with volumes as small as 70 pl, assessing their optical clarity and measuring their buoyancy in liquid nitrogen-argon solutions. The use of these densities in contraction matching of internal solvent to the available solvent spaces is complicated by several factors, most notably the exclusion of cryoprotectants from protein hydration shells and the expected deviation of the contraction behavior of hydration water from bulk water. The present methods and results will assist in developing rational approaches to cryoprotection and an understanding of solvent behavior in protein crystals.
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