title: Optimization of data collection taking radiation damage into account.
abstract: To take into account the effects of radiation damage, new algorithms for the optimization of data-collection strategies have been implemented in the software package BEST. The intensity variation related to radiation damage is approximated by log-linear functions of resolution and cumulative X-ray dose. Based on an accurate prediction of the basic characteristics of data yet to be collected, BEST establishes objective relationships between the accessible data completeness, resolution and signal-to-noise statistics that can be achieved in an experiment and designs an optimal plan for data collection.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85b, 22607 Hamburg, Germany.
authors.forename: Gleb P
authors.initials: GP
authors.lastname: Bourenkov
authors.forename: Alexander N
authors.initials: AN
authors.lastname: Popov
mesh_terms: D000465:Algorithms; D029063:Aquifoliaceae / Q000737:chemistry; D002265:Carboxylic Ester Hydrolases / Q000032:analysis; D048013:Acetivibrio thermocellus / Q000201:enzymology; D018360:Crystallography, X-Ray / Q000379:methods*; D004307:Dose-Response Relationship, Radiation; D007328:Insulin / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D034741:RNA, Small Interfering / Q000032:analysis / Q000737:chemistry; D017864:Tombusvirus / Q000737:chemistry; D014764:Viral Proteins / Q000032:analysis / Q000737:chemistry; D014965:X-Rays
chemical_list: D007328:Insulin; D008565:Membrane Proteins; C493885:P19 protein, tomato bushy stunt virus; D034741:RNA, Small Interfering; D014764:Viral Proteins; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase
references.citation: Acta Crystallogr D Biol Crystallogr. 2008 Feb;64(Pt 2):158-66
references.pmid: 18219115
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):72-82
references.pmid: 16369096
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Curr Opin Struct Biol. 2006 Oct;16(5):624-9
references.pmid: 16938450
references.citation: Structure. 2001 Dec;9(12):1183-90
references.pmid: 11738044
references.citation: Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4912-7
references.pmid: 16549763
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):32-47
references.pmid: 16369092
references.citation: Methods Enzymol. 1997;276:472-494
references.pmid: 27799110
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):58-64
references.pmid: 16369094
references.citation: Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1227-37
references.pmid: 16131756
references.citation: Acta Crystallogr B Struct Crystallogr Cryst Chem. 1970 Jul 15;26(7):998-1004
references.pmid: 5536135
references.citation: Structure. 2003 Jan;11(1):13-9
references.pmid: 12517336
references.citation: Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1030-8
references.pmid: 16929104
references.citation: J Synchrotron Radiat. 2006 May;13(Pt 3):227-38
references.pmid: 16645249
references.citation: J Synchrotron Radiat. 2009 Nov;16(Pt 6):872-9
references.pmid: 19844027
references.citation: Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
references.pmid: 15299926
references.citation: Protein Sci. 2005 Jun;14(6):1498-507
references.pmid: 15883191
references.citation: Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):623-8
references.pmid: 10639129
references.citation: Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):535-42
references.pmid: 19465767
references.citation: Nature. 2003 Dec 18;426(6968):874-8
references.pmid: 14661029
references.citation: Structure. 2000 Mar 15;8(3):315-28
references.pmid: 10745008
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1145-53
references.pmid: 12832757
references.citation: Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):328-41
references.pmid: 10713520