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Article: Measurements of accurate x-ray scattering data of protein solutions using small stationary sample cells

TitleMeasurements of accurate x-ray scattering data of protein solutions using small stationary sample cells
Authors
Issue Date2009
PublisherAmerican Institute of Physics. The Journal's web site is located at http://ojps.aip.org/rsio/
Citation
Review Of Scientific Instruments, 2009, v. 80 n. 1 How to Cite?
AbstractIn this paper, we report a method of precise in situ x-ray scattering measurements on protein solutions using small stationary sample cells. Although reduction in the radiation damage induced by intense synchrotron radiation sources is indispensable for the correct interpretation of scattering data, there is still a lack of effective methods to overcome radiation-induced aggregation and extract scattering profiles free from chemical or structural damage. It is found that radiation-induced aggregation mainly begins on the surface of the sample cell and grows along the beam path; the diameter of the damaged region is comparable to the x-ray beam size. Radiation-induced aggregation can be effectively avoided by using a two-dimensional scan (2D mode), with an interval as small as 1.5 times the beam size, at low temperature (e.g., 4 °C). A radiation sensitive protein, bovine hemoglobin, was used to test the method. A standard deviation of less than 5% in the small angle region was observed from a series of nine spectra recorded in 2D mode, in contrast to the intensity variation seen using the conventional stationary technique, which can exceed 100%. Wide-angle x-ray scattering data were collected at a standard macromolecular diffraction station using the same data collection protocol and showed a good signal/noise ratio (better than the reported data on the same protein using a flow cell). The results indicate that this method is an effective approach for obtaining precise measurements of protein solution scattering. © 2009 American Institute of Physics.
Persistent Identifierhttp://hdl.handle.net/10722/59685
ISSN
2015 Impact Factor: 1.336
2015 SCImago Journal Rankings: 0.571
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
National Science FoundationDMR 0225180
National Institutes of Health through its National Center for Research ResourcesRR-01646
Funding Information:

We would like to thank M. Szebenyi for critical reading of the manuscript and R. Gillilan and A. Woll for their help in the experiment. This work is based on research conducted at the CHESS, which is supported by the National Science Foundation under Award No. DMR 0225180, using the Macromolecular Diffraction at CHESS (MacCHESS) facility, supported by Award No. RR-01646 from the National Institutes of Health through its National Center for Research Resources.

References

 

DC FieldValueLanguage
dc.contributor.authorHong, Xen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-05-31T03:55:13Z-
dc.date.available2010-05-31T03:55:13Z-
dc.date.issued2009en_HK
dc.identifier.citationReview Of Scientific Instruments, 2009, v. 80 n. 1en_HK
dc.identifier.issn0034-6748en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59685-
dc.description.abstractIn this paper, we report a method of precise in situ x-ray scattering measurements on protein solutions using small stationary sample cells. Although reduction in the radiation damage induced by intense synchrotron radiation sources is indispensable for the correct interpretation of scattering data, there is still a lack of effective methods to overcome radiation-induced aggregation and extract scattering profiles free from chemical or structural damage. It is found that radiation-induced aggregation mainly begins on the surface of the sample cell and grows along the beam path; the diameter of the damaged region is comparable to the x-ray beam size. Radiation-induced aggregation can be effectively avoided by using a two-dimensional scan (2D mode), with an interval as small as 1.5 times the beam size, at low temperature (e.g., 4 °C). A radiation sensitive protein, bovine hemoglobin, was used to test the method. A standard deviation of less than 5% in the small angle region was observed from a series of nine spectra recorded in 2D mode, in contrast to the intensity variation seen using the conventional stationary technique, which can exceed 100%. Wide-angle x-ray scattering data were collected at a standard macromolecular diffraction station using the same data collection protocol and showed a good signal/noise ratio (better than the reported data on the same protein using a flow cell). The results indicate that this method is an effective approach for obtaining precise measurements of protein solution scattering. © 2009 American Institute of Physics.en_HK
dc.languageengen_HK
dc.publisherAmerican Institute of Physics. The Journal's web site is located at http://ojps.aip.org/rsio/en_HK
dc.relation.ispartofReview of Scientific Instrumentsen_HK
dc.rightsReview of Scientific Instruments. Copyright © American Institute of Physics.en_HK
dc.titleMeasurements of accurate x-ray scattering data of protein solutions using small stationary sample cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0034-6748&volume=80&spage=014303&epage=&date=2009&atitle=Measurements+of+accurate+x-ray+scattering+data+of+protein+solutions+using+small+stationary+sample+cellsen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1063/1.3069285en_HK
dc.identifier.pmid19191451en_HK
dc.identifier.pmcidPMC2736617-
dc.identifier.scopuseid_2-s2.0-59349087753en_HK
dc.identifier.hkuros155966en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-59349087753&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume80en_HK
dc.identifier.issue1en_HK
dc.identifier.isiWOS:000262966000029-
dc.publisher.placeUnited Statesen_HK
dc.deduplication.noteHao, Qen_US
dc.identifier.scopusauthoridHong, X=7201551709en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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