ArticleActa crystallographica. Section D, Biological crystallography2012
Proline: Mother Nature's cryoprotectant applied to protein crystallography.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Identification of essential genes inMicrobial genomics · 2023Article
- A drug-discovery-oriented non-invasive protocol for protein crystal cryoprotection by dehydration, with application for crystallization screening.Journal of applied crystallography · 2022Article
- Structural basis for the stereospecific inhibition of the dual proline/hydroxyproline catabolic enzyme ALDH4A1 by trans-4-hydroxy-L-proline.Protein science : a publication of the Protein Society · 2021Article
- The Multifaceted Roles of Proline in Cell Behavior.Frontiers in cell and developmental biology · 2021Review
- Autumn shifts in cold tolerance metabolites in overwintering adult mountain pine beetles.PloS one · 2020Article
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Improving Viscosity and Stability of a Highly Concentrated Monoclonal Antibody Solution with Concentrated Proline.Pharmaceutical research · 2018Article
- To Protect and to Preserve: Novel Preservation Strategies for Extracellular Vesicles.Frontiers in pharmacology · 2018Review
- Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline.Molecules (Basel, Switzerland) · 2017Article
- Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.The Journal of biological chemistry · 2017Article
- Practical macromolecular cryocrystallography.Acta crystallographica. Section F, Structural biology communications · 2015Review
- Efficient cryoprotection of macromolecular crystals using vapor diffusion of volatile alcohols.Journal of structural biology · 2014Article
- Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state.Biochemistry · 2014Article
- Structural basis of substrate selectivity of Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length.Archives of biochemistry and biophysics · 2013Article
- Proline mechanisms of stress survival.Antioxidants & redox signaling · 2013Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
L-Proline is one of Mother Nature's cryoprotectants. Plants and yeast accumulate proline under freeze-induced stress and the use of proline in the cryopreservation of biological samples is well established. Here, it is shown that L-proline is also a useful cryoprotectant for protein crystallography. Proline was used to prepare crystals of lysozyme, xylose isomerase, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase for low-temperature data collection. The crystallization solutions in these test cases included the commonly used precipitants ammonium sulfate, sodium chloride and polyethylene glycol and spanned the pH range 4.6-8.5. Thus, proline is compatible with typical protein-crystallization formulations. The proline concentration needed for cryoprotection of these crystals is in the range 2.0-3.0 M. Complete data sets were collected from the proline-protected crystals. Proline performed as well as traditional cryoprotectants based on the diffraction resolution and data-quality statistics. The structures were refined to assess the binding of proline to these proteins. As observed with traditional cryoprotectants such as glycerol and ethylene glycol, the electron-density maps clearly showed the presence of proline molecules bound to the protein. In two cases, histidine acid phosphatase and 1-pyrroline-5-carboxylate dehydrogenase, proline binds in the active site. It is concluded that L-proline is an effective cryoprotectant for protein crystallography.
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