From Screen to Structure with a Harvestable Microfluidic Device

Vivian Stojanoff, Jean Jakoncic, Deena A. Oren, V. Nagarajan, Jens-Christian Navarro Poulsen, Melanie A. Adams-Cioaba, Terese Bergfors, Morten Otto Alexander Sommer

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Advances in automation have facilitated the widespread adoption of highthroughput vapour-diffusion methods for initial crystallization screening. However, for many proteins, screening thousands of crystallization conditions fails to yield crystals of sufficient quality for structural characterization. Here, the rates of crystal identification for thaumatin, catalase and myoglobin using microfluidic Crystal Former devices and sitting-drop vapour-diffusion plates are compared. It is shown that the Crystal Former results in a greater number of identified initial crystallization conditions compared with vapour diffusion. Furthermore, crystals of thaumatin and lysozyme obtained in the Crystal Former were used directly for structure determination both in situ and upon harvesting and cryocooling. On the basis of these results, a crystallization strategy is proposed that uses multiple methods with distinct kinetic trajectories through the protein phase diagram to increase the output of crystallization pipelines.
Original languageEnglish
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
Issue number8
Pages (from-to)971-975
Number of pages5
Publication statusPublished - 2011
Externally publishedYes


  • Crystal Former
  • Protein crystallization
  • Structural biology
  • Liquid-liquid diffusion
  • Microfluidics


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