ArticleActa crystallographica. Section D, Biological crystallography2011
Development of high-performance X-ray transparent crystallization plates for in situ protein crystal screening and analysis.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Efficient in situ screening of and data collection from microcrystals in crystallization plates.Acta crystallographica. Section D, Structural biology · 2024Article
- Novel combined crystallization plate for high-throughput crystal screening and in situ data collection at a crystallography beamline.Acta crystallographica. Section F, Structural biology communications · 2021Article
- The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting.Acta crystallographica. Section D, Structural biology · 2021Article
- Graphene-based microfluidics for serial crystallography.Lab on a chip · 2016Article
- Automated harvesting and processing of protein crystals through laser photoablation.Acta crystallographica. Section D, Structural biology · 2016Article
- Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Identifying, studying and making good use of macromolecular crystals.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Automation in biological crystallization.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Exploiting fast detectors to enter a new dimension in room-temperature crystallography.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Approaches to automated protein crystal harvesting.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Acoustic methods for high-throughput protein crystal mounting at next-generation macromolecular crystallographic beamlines.Journal of synchrotron radiation · 2013Article
- Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography.Acta crystallographica. Section D, Biological crystallography · 2013Article
- In situ macromolecular crystallography using microbeams.Acta crystallographica. Section D, Biological crystallography · 2012Article
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4 authors.
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Abstract
X-ray transparent crystallization plates based upon a novel drop-pinning technology provide a flexible, simple and inexpensive approach to protein crystallization and screening. The plates consist of open cells sealed top and bottom by thin optically, UV and X-ray transparent films. The plates do not need wells or depressions to contain liquids. Instead, protein drops and reservoir solution are held in place by rings with micrometre dimensions that are patterned onto the bottom film. These rings strongly pin the liquid contact lines, thereby improving drop shape and position uniformity, and thus crystallization reproducibility, and simplifying automated image analysis of drop contents. The same rings effectively pin solutions containing salts, proteins, cryoprotectants, oils, alcohols and detergents. Strong pinning by rings allows the plates to be rotated without liquid mixing to 90° for X-ray data collection or to be inverted for hanging-drop crystallization. The plates have the standard SBS format and are compatible with standard liquid-handling robots.
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