dc.contributor.author | King, Gordon J | |
dc.contributor.author | Chen, Kai-En | |
dc.contributor.author | Robin, Gautier | |
dc.contributor.author | Forwood, Jade K | |
dc.contributor.author | Heras, Begona | |
dc.contributor.author | Thakur, Anil S | |
dc.contributor.author | Kobe, Bostjan | |
dc.contributor.author | Blomberg, Simon P | |
dc.contributor.author | Martin, Jennifer L | |
dc.date.accessioned | 2017-09-22T04:26:30Z | |
dc.date.available | 2017-09-22T04:26:30Z | |
dc.date.issued | 2009 | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.doi | 10.1371/journal.pone.0007851 | |
dc.identifier.uri | http://hdl.handle.net/10072/347154 | |
dc.description.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.
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.
Conclusions/Significance: 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. | |
dc.description.peerreviewed | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Public Library of Sciences | |
dc.relation.ispartofpagefrom | e7851-1 | |
dc.relation.ispartofpageto | e7851-5 | |
dc.relation.ispartofissue | 11 | |
dc.relation.ispartofjournal | PLoS One | |
dc.relation.ispartofvolume | 4 | |
dc.subject.fieldofresearch | Biochemistry and cell biology not elsewhere classified | |
dc.subject.fieldofresearchcode | 310199 | |
dc.title | Interaction between plate make and protein in protein crystallisation screening | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
dcterms.license | http://creativecommons.org/licenses/by/4.0/ | |
dc.description.version | Version of Record (VoR) | |
gro.rights.copyright | © 2009 King et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | |
gro.hasfulltext | Full Text | |
gro.griffith.author | Martin, Jennifer | |