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Cited by 517

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion

Open access
Hansen, Carl L., Skordalakes, Emmanuel, Berger, James M., Quake, Stephen R.·2002·Proceedings of the National Academy of Sciences

Abstract

Producing robust and scalable fluid metering in a microfluidic device is a challenging problem. We developed a scheme for metering fluids on the picoliter scale that is scalable to highly integrated parallel architectures and is independent of the properties of the working fluid. We demonstrated the power of this method by fabricating and testing a microfluidic chip for rapid screening of protein crystallization conditions, a major hurdle in structural biology efforts. The chip has 480 active valves and performs 144 parallel reactions, each of which uses only 10 nl of protein sample. The properties of microfluidic mixing allow an efficient kinetic trajectory for crystallization, and the microfluidic device outperforms conventional techniques by detecting more crystallization conditions while using 2 orders of magnitude less protein sample. We demonstrate that diffraction-quality crystals may be grown and harvested from such nanoliter-volume reactions.

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Crossref · 10.1073/pnas.262485199

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Metadata

Authors
Hansen, C. L., Skordalakes, E., Berger, J. M., & Quake, S. R.
Venue
Proceedings of the National Academy of Sciences
Published
2002-12-16
Volume
99
Issue
26
Pages
16531-16536
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2078863041
Cited by
517
References
24
FWCI
22.71
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion. https://app.cochat.ai/papers/10.1073/pnas.262485199
The paper
Hansen, C. L., Skordalakes, E., Berger, J. M., & Quake, S. R. (2002). A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.262485199

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.