ArticleActa crystallographica. Section D, Structural biology2018
The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.Acta crystallographica. Section D, Structural biology · 2026Article
- Direct Measurement of Protein Corona Thickness on Nanomaterials Using Dual-Color Stochastic Optical Reconstruction Microscopy (STORM).Small methods · 2026Article
- The Structural Stability of Enzymatic Proteins in the Gas Phase: A Comparison of Semiempirical Hamiltonians and the GFN-FF.Molecules (Basel, Switzerland) · 2025Article
- Challenges in solving structures from radiation-damaged tomograms of protein nanocrystals assessed by simulation.Acta crystallographica. Section D, Structural biology · 2021Article
- The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting.Acta crystallographica. Section D, Structural biology · 2021Article
- Solvent flows, conformation changes and lattice reordering in a cold protein crystal.Acta crystallographica. Section D, Structural biology · 2019Article
- A comparison of gas stream cooling and plunge cooling of macromolecular crystals.Journal of applied crystallography · 2019Article
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8 authors.
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Abstract
Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling.
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