TheBiophysicalSociety of Japan General IncorporatedAssociation period in-vacuum undulator, high-gradient C-band linac, and a high-quality thermionic electron gun has enabled to decrease the electron beam energy, and to reduce the faciHty sca]e, for preduction even of hard x-ray FEL. The construction of SACLA started in FY2006. Thc first eleetron beam ",as iniectcd in the late ofFebruary, 201 1 . The electron-beam accelcration to 8 GeV, as we[L as the obscrvation of spontafieous x-rays at a

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... ength of O.8 Angstrom, were achieved in March 20l 1. The fact that we have reached lasing afteT ollly three months of etectren bearn commissioning indicates (i) the va]idity of the basic design concept of SCSS (SPring-S Cornpact SASE Seurce) as we]t as the experiencc accuinulated duJ'ing the operation of SCSS prototype machine, (ii) the certainty of the cemponents dcvelopment, design, fabrication, installation, alignment and tune-up and (iii) the adequacy oC the beam commissioning stTategy, ineaning that the project has moved ahead with extraordinaire smoothness. We arc continuing the commissioning of SACLA in order te deliver higher intensity and shorter wavelength X-ray laser with higher stability, SACLA will be open for pubTic users jn March, 2012. ISI-02 IPre.H.tasttI ¢ [[suYUffin.]t-VtzFXan@theeewee;E=ge Coherent X-ray difTtaction microscopy of non-crystalline biological particles at cr.vogenic temperatures Masayoshi Nakasakoi'2, Masaki Yamarnoto2 (iDepartJnent qfPhysics, Kkio Univers'in." ?iUww Sl'ring-8 Cente4 RIKEN Harima tnstitute) CoheTent X-ray diffraction microscopy (CXDM) has appeared as a novel tool for the stnictura] studies of non-crystalline bielogical particles to be never erystallized. This technique uses intense X-ray beams with good transverse coherence from third-generation synchrotron facilities and X-ray fi'ee electron laser (XFEL) sources. The wealc interactions ofX-rays with electrons enable thc penetration into thick sampTes and thc Born approximation in the difftaction process. One ef serious problems in the application is radiatioll damage ef samples. Bccausc of the small scattering cross sections of atoms in biological samples. tong period exposure eausing radiation damage is necessary to collect diffraction data to be analyzed. To overcome radiation damage or biological samples, we recently constructed a system for cryogenic CXDM experiments in X-ray free elcctron laser and the third generation synchrotron t'acilities. HeTe we would likc to introduce our system, in particular on two typcs oCdirn'actometers dedicated for cryogenic CXDM experiments, and preliminary results from cryogenic experiments conducted at BL29XU of SPring-8. We also present the method to Teconstruct 3D clcctron densities of sample particles only from difftactionpatterns. ISI-03 SACLA in Molecular lmaging Changyong Song {RllIEN st]ring-8 Center) X-ray crysta]]ogTephy, for more than fifty years, has been thc prhnary methodology to unveil structures of biological molecules at atomic detajl. Notu,ithstanding the remarkable technieal advancement, structurai investigations of general biological specimens with x-rays have been charTenged, oflen 1iaiiipered by difficulty in making crystals, Alternatively x-ray lens based direct imaging techniques have been developed but the imagc resolution is limited by the focusing capabi1ity oflens itself, The coherent x-ray diffractive imaging technique expeets to provide a breakthrough without relying on either a crysta] or lens. A series ofdcvelopments has matured the teehnique to demonstrate noninvasive 3D {maging ofwhole biological cells and organelles at a few tens ofnanoineter resolution. This imaging techniquc, furthcr with the advent of bright and short-pulse x-ray lasers, aims to rea]ize near atomic rcso]ution 3D imaging of single-macremolecules, In this talk, I wM introduce our reeent progrcss on biological 3D imaging made by using hard x-rays at SPring-8. Current status and perspective ef molecular imaghig with SACLA will alse be discussed. Minerals and metals are essential for a heaTthy body, and the concentrations of these e]ements have been suggcsted to change in various eellular conditions and the diseased state. However. the distribution ofthesc intracellular elements was hardtebevisualized.WedescribethedeveloprnentanduseofascanningX-ray Ruoreseence microscope (SXFM) system at SPring-8 (Harima, Riken) and an accompanying analytical method (elemental array). We demonstrate that a SXFM can reliably determine the cellular distribution ofmultiple elements with a high spatial resolution, Visualizing intracellulur elemerrts and understanding their kineties may provide greater insight into cellular kinetics alld disease etiology. We also discuss the possible application of X-ray fluorescence microscopy to the fourth-generation tight sources, x-ray free electron ]asers. I SF05 X.ray FEL EMLIteeeeefidivaneor X-ray FEL and membrane pTotein crystallography Se Iwata {Dep. Cell Biolog}; G'ad. Schooi ofiLfbd., 1(}'oto Uhiv.) Membrane proteins aTe a supreme example wherc more effort in stmctural biolegy is needed. In spite of their abundance and irnpertance, of the 72,OOO protein structures in the Protein Data Bank, on]y some 2Se ofthese proteins are unique membrane proteins, Many major questions remain unanswered; these include the signal transduction mechanism of G protein coupled receptors (GPCRs), the gating mechauisms of ion channe]s, and the molecular transport mechanism of transporters. Membrane protein struetures are of erucial importance foT medicjne. Historically, the discovery efnew drugs has been led by chemistry and pharmacolegy. The advent ofgenomic scicnces has opened up the possibility of identitication of genetic determinants of difTbrent drug responses across a population and the possibility of drug therapy based on the patient's genetic profile, Structural data can inform library design. Iibrary screening, selection oftaTgets. optimisation of lead compounds, and engineering of sclectivity to improve the overaTl efficiency of drug djseovery, As Chapman and his co]leagues showed in a recent paper (Chapman, H.N. et al., Nature 470, 73 (201O>), Xray FEL has a grcat pot ¢ ntial te solve membrane protein structures using multiple microtnane-crysta]s. [n my talk, t would discuss -'hat we could achievc using SACLA in the fietd of membrane protein crystallography based on our expericnce, particularly on the studies perfornied at the microfocus beamLine I24, Diamond light sourec.