ArticleJournal of applied crystallography2009
Slow cooling of protein crystals.
Article in Journal of applied crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- A structural perspective on the temperature-dependent activity of enzymes.bioRxiv : the preprint server for biology · 2024Article
- Effects of cryo-EM cooling on structural ensembles.Nature communications · 2022Article
- Temperature artifacts in protein structures bias ligand-binding predictions.Chemical science · 2021Article
- Ice in biomolecular cryocrystallography.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
- Article
- Journey to the center of the protein: allostery from multitemperature multiconformer X-ray crystallography.Acta crystallographica. Section D, Structural biology · 2019Article
- 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
- Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography.eLife · 2015Article
- Practical macromolecular cryocrystallography.Acta crystallographica. Section F, Structural biology communications · 2015Review
- Improved reproducibility of unit-cell parameters in macromolecular cryocrystallography by limiting dehydration during crystal mounting.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Approaches to automated protein crystal harvesting.Acta crystallographica. Section F, Structural biology communications · 2014Article
- A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter.Journal of applied crystallography · 2013Article
- Global radiation damage: temperature dependence, time dependence and how to outrun it.Journal of synchrotron radiation · 2013Article
- Spatial distribution of radiation damage to crystalline proteins at 25-300 K.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Global radiation damage at 300 and 260 K with dose rates approaching 1 MGy s⁻¹.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Dark progression reveals slow timescales for radiation damage between T = 180 and 240 K.Acta crystallographica. Section D, Biological crystallography · 2011Article
- Macromolecular crystallography radiation damage research: what's new?Journal of synchrotron radiation · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cryoprotectant-free thaumatin crystals have been cooled from 300 to 100 K at a rate of 0.1 K s(-1) - 10(3)-10(4) times slower than in conventional flash cooling - while continuously collecting X-ray diffraction data, so as to follow the evolution of protein lattice and solvent properties during cooling. Diffraction patterns show no evidence of crystalline ice at any temperature. This indicates that the lattice of protein molecules is itself an excellent cryoprotectant, and with sodium potassium tartrate incorporated from the 1.5 M mother liquor ice nucleation rates are at least as low as in a 70% glycerol solution. Crystal quality during slow cooling remains high, with an average mosaicity at 100 K of 0.2 degrees . Most of the mosaicity increase occurs above approximately 200 K, where the solvent is still liquid, and is concurrent with an anisotropic contraction of the unit cell. Near 180 K a crossover to solid-like solvent behavior occurs, and on further cooling there is no additional degradation of crystal order. The variation of B factor with temperature shows clear evidence of a protein dynamical transition near 210 K, and at lower temperatures the slope dB/dT is a factor of 3-6 smaller than has been reported for any other protein. These results establish the feasibility of fully temperature controlled studies of protein structure and dynamics between 300 and 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.