title: Interaction between plate make and protein in protein crystallisation screening.
abstract: BACKGROUND
  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.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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 crystallize, 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.
authors.affiliation: Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland, Australia.
authors.forename: Gordon J
authors.initials: GJ
authors.lastname: King
authors.forename: Kai-En
authors.initials: KE
authors.lastname: Chen
authors.forename: Gautier
authors.initials: G
authors.lastname: Robin
authors.forename: Jade K
authors.initials: JK
authors.lastname: Forwood
authors.forename: Begoña
authors.initials: B
authors.lastname: Heras
authors.forename: Anil S
authors.initials: AS
authors.lastname: Thakur
authors.forename: Bostjan
authors.initials: B
authors.lastname: Kobe
authors.forename: Simon P
authors.initials: SP
authors.lastname: Blomberg
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Martin
mesh_terms: D000818:Animals; D000941:Antigens / Q000737:chemistry; D002374:Catalase / Q000737:chemistry; D002417:Cattle; D002645:Chickens; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods; D004529:Egg White / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D051379:Mice; D009113:Muramidase / Q000737:chemistry; D010865:Pilot Projects; D011506:Proteins / Q000737:chemistry*; D013302:Streptomyces / Q000378:metabolism
chemical_list: D000941:Antigens; C086812:Lxn protein, rat; D011506:Proteins; D002374:Catalase; D009113:Muramidase