Interaction Between Plate Make And Protein In Protein Crystallisation Screening

Gordon J. King, Kai-En Chen, Gautier Robin, Jade Forwood, Begona Heras, Anil S. Thakur, Bostjan Kobe, Simon P. Blomberg, Jennifer L. Martin

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Protein crystallisation screening involves the parallel testing of large numbers of candidate conditions with the aim of identifying conditions suitable as a starting point for the production of diffraction quality crystals. Generally, condition screening is performed in 96-well plates. While previous studies have examined the effects of protein construct, protein purity, or crystallisation condition ingredients on protein crystallisation, few have examined the effect of the crystallisation plate. We performed a statistically rigorous examination of protein crystallisation, and evaluated interactions between crystallisation success and plate row/column, different plates of same make, different plate makes and different proteins. From our analysis of protein crystallisation, we found a significant interaction between plate make and the specific protein being crystallised. Protein crystal structure determination is the principal method for determining protein structure but is limited by the need to produce crystals of the protein under study. Many important proteins are difficult to crystallise, so that identification of factors that assist crystallisation could open up the structure determination of these more challenging targets. Our findings suggest that protein crystallisation success may be improved by matching a protein with its optimal plate make.
Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume4
Issue number11
DOIs
Publication statusPublished - 2009

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