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Microseed matrix screening for optimization in protein crystallization: what have we learned?
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
2014 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 70, 1117-1126 p.Article in journal (Refereed) Published
Abstract [en]

Protein crystals obtained in initial screens typically require optimization before they are of X-ray diffraction quality. Seeding is one such optimization method. In classical seeding experiments, the seed crystals are put into new, albeit similar, conditions. The past decade has seen the emergence of an alternative seeding strategy: microseed matrix screening (MMS). In this strategy, the seed crystals are transferred into conditions unrelated to the seed source. Examples of MMS applications from in-house projects and the literature include the generation of multiple crystal forms and different space groups, better diffracting crystals and crystallization of previously uncrystallizable targets. MMS can be implemented robotically, making it a viable option for drug-discovery programs. In conclusion, MMS is a simple, time-and cost-efficient optimization method that is applicable to many recalcitrant crystallization problems.

Place, publisher, year, edition, pages
2014. Vol. 70, 1117-1126 p.
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-234157DOI: 10.1107/S2053230X14015507ISI: 000341818600001OAI: oai:DiVA.org:uu-234157DiVA: diva2:755861
Available from: 2014-10-15 Created: 2014-10-14 Last updated: 2017-12-05Bibliographically approved

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Bergfors, Terese

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