Iterative screen optimization maximizes the efficiency of macromolecular crystallization.
Sweet16
automated liquid handling
crystallization screening
macromolecular crystallography
Journal
Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319
Informations de publication
Date de publication:
01 Feb 2019
01 Feb 2019
Historique:
received:
25
09
2018
accepted:
06
12
2018
entrez:
5
2
2019
pubmed:
5
2
2019
medline:
29
5
2019
Statut:
ppublish
Résumé
Advances in X-ray crystallography have streamlined the process of determining high-resolution three-dimensional macromolecular structures. However, a rate-limiting step in this process continues to be the generation of crystals that are of sufficient size and quality for subsequent diffraction experiments. Here, iterative screen optimization (ISO), a highly automated process in which the precipitant concentrations of each condition in a crystallization screen are modified based on the results of a prior crystallization experiment, is described. After designing a novel high-throughput crystallization screen to take full advantage of this method, the value of ISO is demonstrated by using it to successfully crystallize a panel of six diverse proteins. The results suggest that ISO is an effective method to obtain macromolecular crystals, particularly for proteins that crystallize under a narrow range of precipitant concentrations.
Identifiants
pubmed: 30713164
pii: S2053230X18017338
doi: 10.1107/S2053230X18017338
pmc: PMC6360444
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
123-131Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM113132
Pays : United States
Organisme : National Institutes of Health, National Institute of General Medical Sciences
ID : P20GM113132
Organisme : National Institutes of Health, National Institute of General Medical Sciences
ID : T32GM008704
Organisme : National Institutes of Health, National Institute of General Medical Sciences
ID : 532AI007519
Informations de copyright
open access.
Références
Mol Pathol. 2000 Feb;53(1):8-14
pubmed: 10884915
Trends Biochem Sci. 2000 Dec;25(12):637-43
pubmed: 11116192
Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 1):1601-5
pubmed: 12351870
Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54
pubmed: 12393927
J Struct Biol. 2003 Apr;142(1):88-97
pubmed: 12718922
Structure. 2003 Sep;11(9):1061-70
pubmed: 12962625
Protein Sci. 1992 Sep;1(9):1133-43
pubmed: 1304392
Nature. 1958 Mar 8;181(4610):662-6
pubmed: 13517261
Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):414-23
pubmed: 15299395
J Mol Biol. 2007 May 4;368(3):652-65
pubmed: 17362988
J Am Chem Soc. 2008 Oct 29;130(43):14076-7
pubmed: 18831587
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
J Biol Chem. 1946 Jul;164:1-5
pubmed: 20989461
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
J Appl Crystallogr. 2009 Dec 1;42(Pt 6):1035-1042
pubmed: 22477774
Science. 2013 Nov 1;342(6158):592-8
pubmed: 24179220
Acta Crystallogr D Biol Crystallogr. 2014 Oct;70(Pt 10):2702-18
pubmed: 25286854
Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):1036-48
pubmed: 27599736
Acta Crystallogr D Struct Biol. 2017 Mar 1;73(Pt 3):246-255
pubmed: 28291760
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1604-8
pubmed: 3856839
Arch Biochem Biophys. 1972 Aug;151(2):533-9
pubmed: 4625692
Biochemistry. 1972 Dec 19;11(26):4910-9
pubmed: 4638345