Interaction between plate make and protein in protein crystallisation screening

King, Gordon J., Chen, Kai-En, Robin, Gautier, Forwood, Jade K., Heras, Begoña, Thakur, Anil S., Kobe, Bostjan, Blomberg, Simon P. and Martin, Jennifer L. (2009) Interaction between plate make and protein in protein crystallisation screening. PLoS One, 4 11: x-x. doi:10.1371/journal.pone.0007851

Author King, Gordon J.
Chen, Kai-En
Robin, Gautier
Forwood, Jade K.
Heras, Begoña
Thakur, Anil S.
Kobe, Bostjan
Blomberg, Simon P.
Martin, Jennifer L.
Title Interaction between plate make and protein in protein crystallisation screening
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2009-11
Year available 2009
Sub-type Article (original research)
DOI 10.1371/journal.pone.0007851
Open Access Status DOI
Volume 4
Issue 11
Start page x
End page x
Total pages 5
Editor Joel L. Sussman
Place of publication San Francisco, U.S.
Publisher Public Library of Science
Collection year 2010
Language eng
Subject 11 Medical and Health Sciences
920299 Health and Support Services not elsewhere classified
0304 Medicinal and Biomolecular Chemistry
030406 Proteins and Peptides
Formatted 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.

Methodology/Principal Findings

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.
Keyword Protein Crystallization
Protein Crystal Structure
Q-Index Code C1
Q-Index Status Confirmed Code
Additional Notes Article number: e7851

Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sun, 17 Jan 2010, 00:00:51 EST