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Published October 2005 | Accepted Version
Journal Article Open

Using nanoliter plugs in microfluidics to facilitate and understand protein crystallization

Abstract

Protein crystallization is important for determining protein structures by X-ray diffraction. Nanoliter-sized plugs aqueous droplets surrounded by a fluorinated carrier fluid have been applied to the screening of protein crystallization conditions. Preformed arrays of plugs in capillary cartridges enable sparse matrix screening. Crystals grown in plugs inside a microcapillary may be analyzed by in situ X-ray diffraction. Screening using plugs, which are easily formed in PDMS microfluidic channels, is simple and economical, and minimizes consumption of the protein. This approach also has the potential to improve our understanding of the fundamentals of protein crystallization, such as the effect of mixing on the nucleation of crystals.

Additional Information

© 2005 Elsevier. Available online 8 September 2005. The work described in this review has been supported by the National Institute for Biomedical Imaging and Bioengineering (R01 EB001903), by the National Institute of General Medical Sciences and National Center for Research Resources under the PSI-2 Specialized Center program (U54 GM074961), by the Beckman Young Investigator Program and by the DuPont Young Professor Award. We thank Keith Moffat, Chuan He and Phoebe Rice for their help in advancing the work described in this review. We thank our colleagues in the Ismagilov laboratory who have contributed to the work described here, and Peter Kuhn, Ray Stevens and Lance Stewart for helpful discussions.

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August 22, 2023
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