ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Fast high-pressure freezing of protein crystals in their mother liquor.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- A drug-discovery-oriented non-invasive protocol for protein crystal cryoprotection by dehydration, with application for crystallization screening.Journal of applied crystallography · 2022Article
- Nanomedical Relevance of the Intermolecular Interaction Dynamics-Examples from Lysozymes and Insulins.ACS omega · 2019Article
- The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.Acta crystallographica. Section D, Structural biology · 2018Article
- A standardized technique for high-pressure cooling of protein crystals.Acta crystallographica. Section D, Structural biology · 2017Article
- Room-temperature macromolecular crystallography using a micro-patterned silicon chip with minimal background scattering.Journal of applied crystallography · 2016Article
- 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
- Improved reproducibility of unit-cell parameters in macromolecular cryocrystallography by limiting dehydration during crystal mounting.Acta crystallographica. Section D, Biological crystallography · 2014Article
- High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method.Journal of synchrotron radiation · 2013Article
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Authors and funding
9 authors.
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Abstract
High-pressure freezing (HPF) is a method which allows sample vitrification without cryoprotectants. In the present work, protein crystals were cooled to cryogenic temperatures at a pressure of 210 MPa. In contrast to other HPF methods published to date in the field of cryocrystallography, this protocol involves rapid sample cooling using a standard HPF device. The fast cooling rates allow HPF of protein crystals directly in their mother liquor without the need for cryoprotectants or external reagents. HPF was first attempted with hen egg-white lysozyme and cubic insulin crystals, yielding good to excellent diffraction quality. Non-cryoprotected crystals of the membrane protein photosystem II have been successfully cryocooled for the first time. This indicates that the presented HPF method is well suited to the vitrification of challenging systems with large unit cells and weak crystal contacts.
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