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1、Proteinstructuraldynamicsinsolutionunveiledvia100-pstime-resolvedx-rayscatteringHyunSunChoa,1,NaranbaatarDashdorja,1,FriedrichSchottea,1,TimothyGraberb,RobertHenningb,andPhilipAnfinruda,2aLaboratoryofChemicalPhysics,NationalInstituteofDiabetesandDigestiveandKidneyDiseases,NationalInstitutesofHealth
2、,Bethesda,MD20892-0520;andbCenterforAdvancedRadiationSources,UniversityofChicago,Chicago,IL60637CommunicatedbyWilliamA.Eaton,NationalInstitutesofHealth–NationalInstituteofDiabetesandDigestiveandKidneyDiseases,Bethesda,MD,March9,2010(receivedforreviewFebruary8,2010)Wehavedevelopedatime-resolvedx-ray
3、scatteringdiffractometerlimitedtothemillisecondtimescalebythedeadtimeforcapableofprobingstructuraldynamicsofproteinsinsolutionwithstopped-flowmixers(15),butwiththeadventofmicromachined100-pstimeresolution.Thisdiffractometer,developedonthecontinuous-flowrapidmixers,ithasbeenimprovedto∼0.3msID14BBioC
4、ARS(ConsortiumforAdvancedRadiationSources)(16,17).Muchshortertimescalescanbeaccessedwhenthestruc-beamlineattheAdvancedPhotonSource,recordsx-rayscatteringturalchangeistriggeredbyalaserpulse.Indeed,time-resolved−1WAXSofseveraldifferentbiomoleculeshasbeendemonstratedsnapshotsoverabroadrangeofqspanning
5、0.02–2.5Å,therebyprovidingsimultaneouscoverageofthesmall-anglex-rayscatter-withtimeresolutionlimitedbythe150-nslaserpulsedurationing(SAXS)andwide-anglex-rayscattering(WAXS)regions.To(18).Motivatedbythatsuccess,wesoughttoextendtime-demonstrateitscapabilities,wehavetrackedstructuralchangesresolvedx-r
6、ayscatteringintotheSAXSregion,expandtheinmyoglobinasitundergoesaphotolysis-inducedtransitionfromcoveragedeeperintotheWAXSregion,andimprovethetimeitscarbonmonoxyform(MbCO)toitsdeoxyform(Mb).ThoughresolutiontothelimitdictatedbythedurationofthesynchrotronthedifferencesbetweentheMbCOandMbcrystalstructu
7、resx-raypulse.Wereporthereourinitialresultswithatime-resolvedaresmall(rmsd<0.2Å),time-resolvedx-rayscatteringdifferencesx-rayscatteringdiffractometercapableofprobingproteinstruc-recordedover8decadesoftimefr
