Microscale vapour diffusion for protein crystallization

Justyna Korczynska, Ting-Chou Hu, David K. Smith, Joby Jenkins, Rob Lewis, Tom Edwards, Andrzej M. Brzozowski

Research output: Contribution to journalArticlepeer-review

Abstract

The development of new crystallization platforms via the application of high-throughput technologies has delivered a plethora of crystallization plates suitable for robot-driven and manual setups. However, practically all these plates (except for microfluidic channel chips) are based on a very similar design and well (precipitant):drop (protein) volume ratios. A new type of crystallization plate (mu plate) has therefore been developed and tested that still employs the classical vapour-diffusion technique but minimizes the precipitant well volume to 1.2 mu l for a 150 nl protein drop setup. This enables a very significant saving on the total bulk of the crystallization screen, hence allowing the application of new, rare and expensive solutions in automated crystallization-screening procedures. Additionally, owing to the very low drop:well volume ratio, the new mu plate can significantly accelerate the equilibrium time necessary for crystal nucleation and growth, in many cases shortening the high-throughput crystallization screening process to a few hours.

Original languageEnglish
Pages (from-to)1009-1015
Number of pages7
JournalActa Crystallographica. Section D, Biological Crystallography
Volume63
DOIs
Publication statusPublished - Sept 2007

Keywords

  • WATER EQUILIBRATION
  • DEPENDENCE
  • SPACE

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