Publications

Selected Publications with Video Summaries (13)

Fromme, R. et al., 2015. Serial femtosecond crystallography of soluble proteins in lipidic cubic phase. IUCrJ, 2(5), pp.545-551.
Nogly, P. et al., 2015. Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ, 2(2), pp.168-176.
Tenboer, J. et al., 2014. Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science, 346(6214), pp.1242-1246.
Wang, D. et al., 2014. Double-focusing mixing jet for XFEL study of chemical kinetics. J Synchrotron Rad, 21(6), pp.1364-1366.
Liu, H. & Spence, J.C.H., 2014. The indexing ambiguity in serial femtosecond crystallography (SFX) resolved using an expectation maximization algorithm. IUCrJ, 1(6), pp.393-401.
Kupitz, C. et al., 2014. Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser. Nature, 513(7517), pp.261-265.
Hosseinizadeh, A. et al., 2014. High-resolution structure of viruses from random diffraction snapshots. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647), pp.20130326-20130326.
Kirian, R.A. et al., 2014. Phasing coherently illuminated nanocrystals bounded by partial unit cells. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647), pp.20130331-20130331.
Yefanov, O. et al., 2014. Mapping the continuous reciprocal space intensity distribution of X-ray serial crystallography. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647), pp.20130333-20130333.
Pande, K. et al., 2014. Deducing fast electron density changes in randomly orientated uncrystallized biomolecules in a pump-probe experiment. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647), pp.20130332-20130332.
Liu, W. et al., 2013. Serial Femtosecond Crystallography of G Protein-Coupled Receptors. Science, 342(6165), pp.1521-1524.
Abdallah, B.G. et al., 2013. Crystallization of the Large Membrane Protein Complex Photosystem I in a Microfluidic Channel. ACS Nano, 7(12), pp.10534-10543.
Liu, H., Zatsepin, N.A. & Spence, J.C.H., 2013. Ab-initio phasing using nanocrystal shape transforms with incomplete unit cells . IUCrJ, 1(1), pp.19-27.

BioXFEL Sponsored Publications (279)

* = Publication cites funding from NSF-STC 'Biology with X-ray Lasers' (NSF-1231306) (76)

Lawrence, R.M., Zook, J.D. & Hogue, B.G., 2016. Full inactivation of alphaviruses in single particle and crystallized forms. Journal of Virological Methods.
Nelson, G. et al., 2016. Three-dimensional-printed gas dynamic virtual nozzles for x-ray laser sample delivery. Optics Express, 24(11), p.11515.
Dörner, K. et al., 2016. Characterization of protein nanocrystals based on the reversibility of crystallization. Crystal Growth & Design.
Martin-Garcia, J.M. et al., 2016. Review: Serial femtosecond crystallography: A revolution in structural biology. Archives of Biochemistry and Biophysics.
Hutchison, C.D.M. et al., 2016. Photocycle Populations with Femtosecond Excitation of Crystalline Photoactive Yellow Protein. Chemical Physics Letters.
Fung, R. et al., 2016. Dynamics from noisy data with extreme timing uncertainty. Nature, 532(7600), pp.471-475.
Chen, Y. & Pollack, L., 2016. SAXS studies of RNA: structures, dynamics, and interactions with partners. WIREs RNA.
Zhou, X.E. et al., 2016. X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex. Sci. Data, 3, p.160021.
White, T.A. et al., 2016. Recent developments in CrystFEL . J Appl Crystallogr, 49(2), pp.680-689.
Coleman, M.A. et al., 2016. Expression and Association of the Yersinia pestis Translocon Proteins, YopB and YopD, Are Facilitated by Nanolipoprotein Particles M. Skurnik, ed. PLoS ONE, 11(3), p.e0150166.
Kessans, S.A. et al., 2016. Immunological Characterization of Plant-Based HIV-1 Gag/Dgp41 Virus-Like Particles M. L. Alvarez, ed. PLoS ONE, 11(3), p.e0151842.
Awel, S. et al., 2016. Visualizing aerosol-particle injection for diffractive-imaging experiments. Optics Express, 24(6), p.6507.
Abdallah, B.G. et al., 2016. Protein Crystallization in an Actuated Microfluidic Nanowell Device. Crystal Growth & Design.
Hansen, D.T. et al., 2016. Polyclonal Antibody Production for Membrane Proteins via Genetic Immunization. Scientific Reports, 6, p.21925.
Han, L. et al., 2016. Loop dynamics of thymidine diphosphate-rhamnose 3?-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis. Structural Dynamics, 3(1), p.012004.
Lee, M.-Y. et al., 2016. Structural Studies of the Human Kappa Opioid Receptor Active State Conformations. Biophysical Journal, 110(3), p.38a-39a.
Ishchenko, A., Cherezov, V. & Liu, W., 2016. Preparation and Delivery of Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography. Biophysical Journal, 110(3), p.59a.
Frank, J. & Ourmazd, A., 2016. Continuous Changes in Structure Mapped by Manifold Embedding of Single-Particle Data in Cryo-EM. Methods.
Ayyer, K. et al., 2016. Macromolecular diffractive imaging using imperfect crystals - Bragg data.
Ayyer, K. et al., 2016. Macromolecular diffractive imaging using imperfect crystals. Nature, 530(7589), pp.202-206.
Ding, J. et al., 2016. Concentration of Sindbis virus with optimized gradient insulator-based dielectrophoresis. Analyst.
Cimermancic, P. et al., 2016. CryptoSite: Expanding the Druggable Proteome by Characterization and Prediction of Cryptic Binding Sites. Journal of Molecular Biology, 428(4), pp.709-719.
Ferguson, K.R. et al., 2016. Transient lattice contraction in the solid-to-plasma transition. Science Advances, 2(1), pp.e1500837-e1500837.
Bajt, S. et al., 2016. One dimensional focusing with high numerical aperture multilayer Laue lens.
Kirian, R.A. & Chapman, H.N., 2015. Imaging of Objects by Coherent Diffraction of X-Ray Free-Electron Laser Pulses. Synchrotron Light Sources and Free-Electron Lasers, pp.1-55.
Gorkhover, T. et al., 2016. Femtosecond and nanometre visualization of structural dynamics in superheated nanoparticles. Nature Photon, 10(2), pp.93-97.
Coe, J. & Fromme, P., 2016. Serial femtosecond crystallography opens new avenues for Structural Biology. PPL, 23(3), pp.255-272.
Jakobi, A.J. et al., 2016. In cellulo serial crystallography of alcohol oxidase crystals inside yeast cells . IUCrJ, 3(2).
Altan, I., Charbonneau, P. & Snell, E.H., 2016. Computational crystallization. Archives of Biochemistry and Biophysics.
Van Benschoten, A.H., Wall, M.E. & Fraser, J.S., 2016. Isotropic Trypsin Model for Comparison of Diffuse Scattering.
Chavas, L.M.G. et al., 2015. Serial femtosecond crystallography on in vivo grown crystals at SACLA - developments and results . Acta Cryst Sect A Found Adv, 71(a1), pp.s148-s148.
Monteiro, D.C.F. et al., 2015. Towards a generalised approach for the time-resolved crystallographic study of enzymes. Acta Cryst Sect A Found Adv, 71(a1), pp.s25-s25.
Chen, J.P.J. et al., 2015. Phase retrieval for randomly terminated finite crystals. Acta Cryst Sect A Found Adv, 71(a1), pp.s17-s17.
Ayyer, K. et al., 2015. Improving resolution in serial crystallography. Acta Cryst Sect A Found Adv, 71(a1), pp.s16-s16.
Schneider, T.R. et al., 2015. Serial synchrotron crystallography experiments at EMBL beamline P14 at PETRA III. Acta Cryst Sect A Found Adv, 71(a1), pp.s12-s12.
Li, D. et al., 2015. Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nat Comms, 6, p.10140.
Eckerskorn, N. et al., 2015. Optically Induced Forces Imposed in an Optical Funnel on a Stream of Particles in Air or Vacuum. Physical Review Applied, 4(6).
Schmidt, M., 2015. Time-Resolved Crystallography at X-ray Free Electron Lasers and Synchrotron Light Sources. Synchrotron Radiation News, 28(6), pp.25-30.
Beyerlein, K.R. et al., 2015. Ceramic micro-injection molded nozzles for serial femtosecond crystallography sample delivery. Review of Scientific Instruments, 86(12), p.125104.
Van Benschoten, A.H. et al., 2015. Measuring and modeling diffuse scattering in protein X-ray crystallography.
Helmich, K.E. et al., 2015. Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of ?-Aryl Ether Bonds in Lignin. J. Biol. Chem., 291(10), pp.5234-5246.
Baxter, E.L. et al., 2016. High-density grids for efficient data collection from multiple crystals. Acta Crystallogr Sect D Struct Biol, 72(1), pp.2-11.
Sierra, R.G. et al., 2015. Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II. Nat Meth.
Fromme, P., 2015. XFELs open a new era in structural chemical biology. Nat Chem Biol, 11(12), pp.895-899.
Sierra, R.G. et al., 2015. Ambient-temperature crystal structure of 30S ribosomal subunit from Thermus thermophilus in complex with paromomycin.
Gan, L., Camacho-Alanis, F. & Ros, A., 2015. Polarizability of Six-Helix Bundle and Triangle DNA Origami and Their Escape Characteristics from a Dielectrophoretic Trap. Anal. Chem., 87(24), pp.12059-12064.
Kupitz, C. et al., 2015. Serial Time resolved crystallography of Photosystem II using a femtosecond X-ray laser. The S state after two flashes (S3).
Thomaston, J.L. et al., 2015. High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction. Proc Natl Acad Sci USA, 112(46), pp.14260-14265.
Rudolf, J.D. et al., 2015. Crystal Structure of the Zorbamycin-Binding Protein ZbmA, the Primary Self-Resistance Element in Streptomyces flavoviridis ATCC21892 . Biochemistry, 54(45), pp.6842-6851.
Keedy, D.A., Fraser, J.S. & van den Bedem, H., 2015. Exposing Hidden Alternative Backbone Conformations in X-ray Crystallography Using qFit A. Shehu, ed. PLoS Comput Biol, 11(10), p.e1004507.
Yefanov, O. et al., 2015. Accurate determination of segmented X-ray detector geometry. Optics Express, 23(22), p.28459.
Miller, R.L. et al., 2015. The crystal structure of nociceptin/orphanin FQ peptide receptor (NOP) in complex with C-35 (PSI Community Target).
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 100 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 150 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 180 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 240 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 260 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 280 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 300 K.
Keedy, D.A. et al., 2015. Multiconformer synchrotron model of CypA at 310 K.
Keedy, D.A. et al., 2015. Multiconformer fixed-target X-ray free electron (XFEL) model of CypA at 273 K.
Zhang, H. et al., 2015. Crystal Structure of Human Angiotensin Receptor in Complex with Inverse Agonist Olmesartan at 2.8A resolution.
Kirian, R.A. & Chapman, H.N., 2015. Imaging of Objects by Coherent Diffraction of X-Ray FEL Pulses. Synchrotron Light Sources and Free-Electron Lasers, pp.1-55.
Keedy, D.A. et al., 2015. Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography. eLife, 4.
Zhang, H. et al., 2015. Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor. J. Biol. Chem., 290(49), pp.29127-29139.
Galli, L. et al., 2015. Towards phasing using high X-ray intensity. IUCrJ, 2(6), pp.627-634.
Robinson, P.J. et al., 2015. Molecular architecture of the yeast Mediator complex. eLife, 4.
Spence, J.C.H., Subramanian, G. & Musumeci, P., 2015. Hollow cone illumination for fast TEM, and outrunning damage with electrons. Journal of Physics B: Atomic, Molecular and Optical Physics, 48(21), p.214003.
Kierspel, T. et al., 2015. Strongly aligned gas-phase molecules at free-electron lasers. Journal of Physics B: Atomic, Molecular and Optical Physics, 48(20), p.204002.
Wierzchowski, W. et al., 2015. Synchrotron topographic evaluation of strain around craters generated by irradiation with X-ray pulses from free electron laser with different intensities. Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, 364, pp.20-26.
Rodriguez, J.A. et al., 2015. MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease protein, alpha-synuclein residues 47-56.
Rodriguez, J.A. et al., 2015. Structure of the toxic core of ?-synuclein from invisible crystals. Nature, 525(7570), pp.486-490.
Hoszowska, J. et al., 2015. X-ray two-photon absorption with high fluence XFEL pulses. Journal of Physics: Conference Series, 635(10), p.102009.
Wang, R.Y.-R. et al., 2015. Structure of the capsaicin receptor, TRPV1, determined by single particle electron cryo-microscopy.
Fuchs, M. et al., 2015. Anomalous nonlinear X-ray Compton scattering. Nature Physics, 11(11), pp.964-970.
Eckerskorn, N. et al., 2015. Toward steering a jet of particles into an x-ray beam with optically induced forces K. Dholakia & G. C. Spalding, eds. Optical Trapping and Optical Micromanipulation XII.
Rodriguez, J.A. et al., 2015. Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 68-78, determined by electron diffraction.
Gong, Z. et al., 2015. Biophysical Characterization of a Vaccine Candidate against HIV-1: The Transmembrane and Membrane Proximal Domains of HIV-1 gp41 as a Maltose Binding Protein Fusion A. Kumar, ed. PLoS ONE, 10(8), p.e0136507.
Lawrence, R.M. et al., 2015. Serial femtosecond X-ray diffraction of enveloped virus microcrystals. Structural Dynamics, 2(4), p.041720.
Abdallah, B.G. et al., 2015. Microfluidic sorting of protein nanocrystals by size for X-ray free-electron laser diffraction. Structural Dynamics, 2(4), p.041719.
Fromme, R. et al., 2015. Serial Femtosecond Crytallography of Soluble Proteins in Lipidic Cubic Phase (C-Phycocyanin from T. elongatus).
Barad, B.A. et al., 2015. EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat Meth, 12(10), pp.943-946.
Fromme, R., Basu, S. & Fromme, P., 2015. Phycocyanin structure from T. elongatus at 2.5-A from XFEL using a viscous delivery medium for serial femtosecond crystallography.
Fromme, R. et al., 2015. Structure of HEWL using Serial Femtosecond Crystallography of Soluble Proteins in Lipidic Cubic Phase.
Fromme, R. et al., 2015. Serial femtosecond crystallography of soluble proteins in lipidic cubic phase. IUCrJ, 2(5), pp.545-551.
Singh, S. et al., 2015. Structural Characterization of CalS8, a TDP-?-d-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis. J. Biol. Chem., 290(43), pp.26249-26258.
Kang, Y. et al., 2015. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.
Van Benschoten, A.H. et al., 2015. Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles. Acta Crystallogr D, 71(8), pp.1657-1667.
Urzhumtsev, A. et al., 2015. From deep TLS validation to ensembles of atomic models built from elemental motions. Acta Crystallogr D, 71(8), pp.1668-1683.
Kang, Y. et al., 2015. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature, 523(7562), pp.561-567.
Goyal, S. et al., 2015. Confirmation of TTC8 as a disease gene for nonsyndromic autosomal recessive retinitis pigmentosa (RP51) . Clinical Genetics, 89(4), pp.454-460.
Galli, L. et al., 2015. Crystal Structure of Gadolinium derivative of HEWL solved using Free-Electron Laser radiation.
Galli, L. et al., 2015. Crystal Structure of Gadolinium derivative of HEWL solved using Free-Electron Laser radiation.
Galli, L. et al., 2015. Crystal Structure of Gadolinium derivative of HEWL solved using intense Free-Electron Laser radiation.
Laksmono, H. et al., 2015. Anomalous Behavior of the Homogeneous Ice Nucleation Rate in "No-Man's Land." The Journal of Physical Chemistry Letters, 6(14), pp.2826-2832.
Mucke, M. et al., 2015. Covariance mapping of two-photon double core hole states in C2H2and C2H6produced by an x-ray free electron laser. New J. Phys., 17(7), p.073002.
Hattne, J. et al., 2015. Corrigendum: Accurate macromolecular structures using minimal measurements from X-ray free-electron lasers. Nat Meth, 12(7), pp.692-692.
Conrad, C.E. et al., 2015. A novel inert crystal delivery medium for serial femtosecond crystallography. IUCrJ, 2(4), pp.421-430.
Pawate, A.S. et al., 2015. Towards time-resolved serial crystallography in a microfluidic device. Acta Crystallogr Sect F Struct Biol Cryst Commun, 71(7), pp.823-830.
Wu, W. et al., 2015. Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser. Acta Crystallogr Sect F Struct Biol Cryst Commun, 71(7), pp.856-860.
Feld, G.K. et al., 2015. Low- Z polymer sample supports for fixed-target serial femtosecond X-ray crystallography . J Appl Crystallogr, 48(4), pp.1072-1079.
Kirian, R.A. et al., 2015. Simple convergent-nozzle aerosol injector for single-particle diffractive imaging with X-ray free-electron lasers. Structural Dynamics, 2(4), p.041717.
Poon, H.C. & Saldin, D.K., 2015. Use of triple correlations for the sign determinations of expansion coefficients of symmetric approximations to the diffraction volumes of regular viruses. Structural Dynamics, 2(4), p.041716.
Li, C., Schmidt, K. & Spence, J.C., 2015. Data collection strategies for time-resolved X-ray free-electron laser diffraction, and 2-color methods. Structural Dynamics, 2(4), p.041714.
Bublitz, M. et al., 2015. Structural studies of P-type ATPase-ligand complexes using an X-ray free-electron laser. IUCrJ, 2(4), pp.409-420.
Singh, S. et al., 2015. Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis. Proteins: Structure, Function, and Bioinformatics, 83(8), pp.1547-1554.
Bublitz, M. et al., 2015. Crystal structure of the SR Ca2+-ATPase in the Ca2-E1-MgAMPPCP form determined by serial femtosecond crystallography using an X-ray free-electron laser.
Clark, J.N. et al., 2015. Imaging transient melting of a nanocrystal using an X-ray laser. Proc Natl Acad Sci USA, 112(24), pp.7444-7448.
Prasciolu, M. et al., 2015. Extended asymmetric-cut multilayer X-ray gratings. Optics Express, 23(12), p.15195.
Wang, F. et al., 2015. Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases. ACS Chemical Biology, 10(9), pp.2048-2056.
Fischer, M., Shoichet, B.K. & Fraser, J.S., 2015. One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites. ChemBioChem, 16(11), pp.1560-1564.
Zook, J. et al., 2015. NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins. Structure, 23(6), pp.1116-1122.
Boutet, S. et al., 2015. Hen egg-white lysozyme structure from a spent-beam experiment at LCLS: original beam.
Boutet, S. et al., 2015. Hen egg-white lysozyme structure from a spent-beam experiment at LCLS: refocused beam.
Keedy, D.A. et al., 2015. High-resolution multiconformer synchrotron model of CypA at 273 K.
Luft, J.R. et al., 2015. The detection and subsequent volume optimization of biological nanocrystals. Structural Dynamics, 2(4), p.041710.
Chavas, L.M.G., Gumprecht, L. & Chapman, H.N., 2015. Possibilities for serial femtosecond crystallography sample delivery at future light sourcesa). Structural Dynamics, 2(4), p.041709.
Yang, J.-H. et al., 2015. Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum. Protein Expression and Purification, 114, pp.1-8.
Schmidt, M. et al., 2015. Room temperature structures beyond 1.5 Å by serial femtosecond crystallography. Structural Dynamics, 2(4), p.041708.
Helml, W. et al., 2015. Sub-Femtosecond Free-Electron Laser Pulses. CLEO: 2015.
Fromme, R. et al., 2015. Light Harvesting Protein Phycocyanin in high resolution using a femtosecond X-Ray laser.
Keedy, D.A., Fraser, J. & van den Bedem, H., 2015. Exposing hidden alternative backbone conformations in X-ray crystallography using qFit.
Hosseinizadeh, A. et al., 2015. Single-particle structure determination by X-ray free-electron lasers: Possibilities and challenges. Structural Dynamics, 2(4), p.041601.
Galli, L. et al., 2015. Electronic damage in S atoms in a native protein crystal induced by an intense X-ray free-electron laser pulse. Structural Dynamics, 2(4), p.041703.
Kim, D.J. et al., 2015. Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP . Proteins: Structure, Function, and Bioinformatics, 83(7), pp.1368-1373.
Zhang, H. et al., 2015. Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography. Cell, 161(4), pp.833-844.
Terwilliger, T.C. et al., 2015. Structure determination with weak anomalous signal.
Auldridge, M.E. et al., 2015. LucY: A Versatile New Fluorescent Reporter Protein S. W. Michnick, ed. PLoS ONE, 10(4), p.e0124272.
Monteiro, D.C.F. et al., 2015. The Structure of the PanD/PanZ Protein Complex Reveals Negative Feedback Regulation of Pantothenate Biosynthesis by Coenzyme A. Chemistry & Biology, 22(4), pp.492-503.
Zhang, H. et al., 2015. XFEL structure of human Angiotensin Receptor.
Aquila, A. et al., 2015. The linac coherent light source single particle imaging road map. Structural Dynamics, 2(4), p.041701.
Coe, J. et al., 2015. Crystallization of Photosystem II for Time-Resolved Structural Studies Using an X-ray Free Electron Laser. Membrane Proteins--Engineering, Purification and Crystallization, pp.459-482.
Ferguson, K.R. et al., 2015. The Atomic, Molecular and Optical Science instrument at the Linac Coherent Light Source. J Synchrotron Rad, 22(3), pp.492-497.
Sophia Weerth, R. et al., 2015. Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution . Proteins: Structure, Function, and Bioinformatics, 83(5), pp.1003-1003.
Liang, M. et al., 2015. The Coherent X-ray Imaging instrument at the Linac Coherent Light Source. J Synchrotron Rad, 22(3), pp.514-519.
Pande, K. et al., 2015. Simulations on time-resolved structure determination of uncrystallized biomolecules in the presence of shot noise. Structural Dynamics, 2(2), p.024103.
Boutet, S. et al., 2015. Characterization and use of the spent beam for serial operation of LCLS. J Synchrotron Rad, 22(3), pp.634-643.
Feng, Y. et al., 2015. Demonstration of simultaneous experiments using thin crystal multiplexing at the Linac Coherent Light Source. J Synchrotron Rad, 22(3), pp.626-633.
Aceti, D.J. et al., 2015. Expression platforms for producing eukaryotic proteins: a comparison of E. coli cell-based and wheat germ cell-free synthesis, affinity and solubility tags, and cloning strategies. Journal of Structural and Functional Genomics, 16(2), pp.67-80.
Chen, J. et al., 2015. Critical assessment of the emission spectra of various photosystem II core complexes. Photosynthesis Research, 124(3), pp.253-265.
Van den Bedem, H. & Fraser, J.S., 2015. Integrative, dynamic structural biology at atomic resolution--it's about time. Nat Meth, 12(4), pp.307-318.
Zhang, D. et al., 2015. Two disparate ligand-binding sites in the human P2Y1 receptor. Nature, 520(7547), pp.317-321.
Traeger, L.L. et al., 2015. Unique patterns of transcript and miRNA expression in the South American strong voltage electric eel (Electrophorus electricus). BMC Genomics, 16(1).
Ginn, H.M. et al., 2015. Structure of Uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 100 K.
Ginn, H.M. et al., 2015. Structure of Uranotaenia sapphirina cypovirus (CPV17) polyhedrin at 298 K.
Monteiro, D.C.F. et al., 2015. Direct visualisation of strain-induced protein post-translational modification.
Monteiro, D.C.F. et al., 2015. Direct visualisation of strain-induced protein prost-translational modification.
Monteiro, D.C.F. et al., 2015. Direct visualisation of strain-induced protein post-translational modification.
Fenalti, G. et al., 2015. Fluorescence Recovery After Photobleaching in Lipidic Cubic Phase (LCP-FRAP). Membrane Proteins--Engineering, Purification and Crystallization, pp.417-437.
Abdallah, B.G. et al., 2015. High Throughput Protein Nanocrystal Fractionation in a Microfluidic Sorter. Anal. Chem., 87(8), pp.4159-4167.
Keedy, D.A. et al., 2015. Mapping the Conformational Landscape of a Dynamic Enzyme by XFEL and Multitemperature Crystallography.
Heifetz, A. et al., 2015. GPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1-2 September 2014. Naunyn-Schmiedeberg's Arch Pharmacol, 388(8), pp.883-903.
Prasciolu, M. et al., 2015. Fabrication of wedged multilayer Laue lenses. Opt. Mater. Express, 5(4), p.748.
Ginn, H.M. et al., 2015. Structure of CPV17 polyhedrin determined by the improved analysis of serial femtosecond crystallographic data. Nat Comms, 6, p.6435.
Gruner, S.M. & Lattman, E.E., 2015. Biostructural Science Inspired by Next-Generation X-Ray Sources. Annual Review of Biophysics, 44(1), pp.33-51.
Ekeberg, T. et al., 2015. Three-Dimensional Reconstruction of the Giant Mimivirus Particle with an X-Ray Free-Electron Laser. Physical Review Letters, 114(9).
Soragni, A. et al., 2015. Toxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation. Molecular Cell, 57(6), pp.1011-1021.
Camacho-Alanis, F. & Ros, A., 2015. Protein dielectrophoresis and the link to dielectric properties. Bioanalysis, 7(3), pp.353-371.
Nogly, P. et al., 2015. Room temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation.
Fischer, M. & Fraser, J.S., 2015. CcP gateless cavity.
Fischer, M. & Fraser, J.S., 2015. CcP gateless cavity.
Fischer, M. & Fraser, J.S., 2015. CcP gateless cavity.
Fischer, M. & Fraser, J.S., 2015. CcP gateless cavity.
Nass, K. et al., 2015. Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams. J Synchrotron Rad, 22(2), pp.225-238.
Fenalti, G. et al., 2015. Structural basis for bifunctional peptide recognition at human ?-opioid receptor. Nature Structural & Molecular Biology, 22(3), pp.265-268.
Kirian, R.A. et al., 2015. Direct Phasing of Finite Crystals Illuminated with a Free-Electron Laser. Physical Review X, 5(1).
Van der Schot, G. et al., 2015. Imaging single cells in a beam of live cyanobacteria with an X-ray laser. Nat Comms, 6, p.5704.
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