Publications

Selected Publications with Video Summaries (18)

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 crystallography of soluble proteins in lipidic cubic phase. IUCrJ, 2(5), pp.545-551.
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.
Schmidt, M. et al., 2015. Room temperature structures beyond 1.5 Ă... by serial femtosecond crystallography. Structural Dynamics, 2(4), p.041708.
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.
Arnlund, D. et al., 2014. Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser. Nature Methods, 11(9), pp.923-926.
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.
Weierstall, U. et al., 2014. Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography. Nat Comms, 5.
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.
Poon, H.-C., Schmidt, M. & Saldin, D.K., 2013. Extraction of Fast Changes in the Structure of a Disordered Ensemble of Photoexcited Biomolecules. Advances in Condensed Matter Physics, 2013, pp.1-5.

BioXFEL Sponsored Publications - (438)

* = Publication cites funding from NSF-STC 'Biology with X-ray Lasers' (NSF-1231306) - (148)

Li, X. et al., 2017. Diffraction data of core-shell nanoparticles from an X-ray free electron laser. Scientific Data, 4, p.170048.
Daurer, B.J. et al., 2017. Experimental strategies for imaging bioparticles with femtosecond hard X-ray pulses. IUCrJ, 4(3).
Zhang, H. et al., 2017. Structural basis for selectivity and diversity in angiotensin II receptors. Nature, 544(7650), pp.327-332.
Lorch, Y. & Kornberg, R.D., 2017. Chromatin-remodeling for transcription. Quarterly Reviews of Biophysics, 50.
Oberthuer, D. et al., 2017. Double-flow focused liquid injector for efficient serial femtosecond crystallography. Scientific Reports, 7, p.44628.
Niessen, K.A. et al., 2017. Moving in the Right Direction: Protein Vibrational Steering Function. Biophysical Journal, 112(5), pp.933-942.
Fuller, F.D. et al., 2017. Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nature Methods, 14(4), pp.443-449.
Standfuss, J. & Spence, J., 2017. Serial crystallography at synchrotrons and X-ray lasers. IUCrJ, 4(2), pp.100-101.
Kim, S.K. et al., 2017. An Engineered TGF-β Monomer that Functions as a Dominant Negative to Block TGF-β Signaling. Journal of Biological Chemistry, p.jbc.M116.768754.
Deb, A. et al., 2017. Bacterial expression, correct membrane targeting and functional folding of the HIV-1 membrane protein Vpu using a periplasmic signal peptide M. Schindler, ed. PLOS ONE, 12(2), p.e0172529.
Samuel, P.P. et al., 2017. Mechanism of Human Apohemoglobin Unfolding. Biochemistry, 56(10), pp.1444-1459.
Guo, H.-F. et al., 2017. A scalable lysyl hydroxylase 2 expression system and luciferase-based enzymatic activity assay. Archives of Biochemistry and Biophysics, 618, pp.45-51.
Plumridge, A. et al., 2017. The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Research.
Gati, C. et al., 2017. Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser. Proceedings of the National Academy of Sciences, 114(9), pp.2247-2252.
De la Cruz, M.J. et al., 2017. Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. Nature Methods, 14(4), pp.399-402.
Elshahawi, S.I. et al., 2017. Structure and specificity of a permissive bacterial C-prenyltransferase. Nature Chemical Biology, 13(4), pp.366-368.
Aboualizadeh, E. et al., 2017. Retinal oxidative stress at the onset of diabetes determined by synchrotron FTIR widefield imaging: towards diabetes pathogenesis. The Analyst, 142(7), pp.1061-1072.
Babcock, N.S. et al., 2017. Model Comparison to Identify Structural Heterogeneity in Protein X-Ray Crystallography. Biophysical Journal, 112(3), p.486a.
Schmidt, M., 2017. A short history of structure based research on the photocycle of photoactive yellow protein. Structural Dynamics, 4(3), p.032201.
Nagai, S. et al., 2017. Chromatin potentiates transcription. Proceedings of the National Academy of Sciences, 114(7), pp.1536-1541.
Adolph, M.B. et al., 2017. Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization. Nucleic Acids Research, 45(6), pp.3378-3394.
Katz, A.M. et al., 2017. Spermine Condenses DNA, but Not RNA Duplexes. Biophysical Journal, 112(1), pp.22-30.
Hughes, R.R. et al., 2017. OleD Loki as a Catalyst for Tertiary Amine and Hydroxamate Glycosylation. ChemBioChem, 18(4), pp.363-367.
Chen, Y. et al., 2016. Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the histone core. Proceedings of the National Academy of Sciences, 114(2), pp.334-339.
Russi, S. et al., 2017. Conformational variation of proteins at room temperature is not dominated by radiation damage. Journal of Synchrotron Radiation, 24(1), pp.73-82.
Kupitz, C. et al., 2017. Structural enzymology using X-ray free electron lasers. Structural Dynamics, 4(4), p.044003.
Plumridge, A., Meisburger, S.P. & Pollack, L., 2016. Visualizing single-stranded nucleic acids in solution. Nucleic Acids Research, p.gkw1297.
Jones, P.V., Salmon, G.L. & Ros, A., 2017. Continuous Separation of DNA Molecules by Size Using Insulator-Based Dielectrophoresis. Analytical Chemistry, 89(3), pp.1531-1539.
Zheng, Y. et al., 2016. Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists. Nature, 540(7633), pp.458-461.
Fromme, P. & Sali, A., 2016. Editorial overview: Biophysical and molecular biological methods. Current Opinion in Structural Biology, 40, pp.ix-xi.
Young, I.D. et al., 2016. Structure of photosystem II and substrate binding at room temperature. Nature, 540(7633), pp.453-457.
Kabanova, V. et al., 2016. Simulations of single-pulse Laue diffraction from proteins with radiation from synchrotron and XFEL sources. Acta Crystallographica Section A Foundations and Advances, 72(a1), pp.s142-s142.
Nogly, P. et al., 2016. Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Acta Crystallographica Section A Foundations and Advances, 72(a1), pp.s41-s42.
Bruno, A.E. et al., 2016. The use of haptic interfaces and web services in crystallography: an application for a `screen to beam' interface. Journal of Applied Crystallography, 49(6), pp.2082-2090.
Stagno, J.R. et al., 2016. Structures of riboswitch RNA reaction states by mix-and-inject XFEL serial crystallography. Nature, 541(7636), pp.242-246.
Hunter, M.S. et al., 2016. Selenium single-wavelength anomalous diffraction de novo phasing using an X-ray-free electron laser. Nature Communications, 7, p.13388.
Zuo, J.M. & Spence, J.C.H., 2017. Advanced Transmission Electron Microscopy.
Edlund, P. et al., 2016. The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Scientific Reports, 6(1).
Biel, J.T. et al., 2016. Flexibility and design: conformational heterogeneity along the evolutionary trajectory of a redesigned ubiquitin.
Lyubimov, A.Y. et al., 2016. Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex. eLife, 5.
Xiang, J. et al., 2016. Successful Strategies to Determine High-Resolution Structures of GPCRs. Trends in Pharmacological Sciences, 37(12), pp.1055-1069.
Chen, J.P.J. et al., 2016. Reconstruction of an object from diffraction intensities averaged over multiple object clusters. Journal of Optics, 18(11), p.114003.
Colletier, J.-P. et al., 2016. De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure. Nature, 539(7627), pp.43-47.
Mendez, D. et al., 2016. Angular correlations of photons from solution diffraction at a free-electron laser encode molecular structure. IUCrJ, 3(6), pp.420-429.
Batyuk, A. et al., 2016. Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Science Advances, 2(9), pp.e1600292-e1600292.
Herascu, N. et al., 2016. Spectral Hole Burning in Cyanobacterial Photosystem I with P700 in Oxidized and Neutral States. The Journal of Physical Chemistry B, 120(40), pp.10483-10495.
Ishchenko, A., Cherezov, V. & Liu, W., 2016. Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography. Journal of Visualized Experiments, (115).
Szlachetko, J. et al., 2016. Establishing nonlinearity thresholds with ultraintense X-ray pulses. Scientific Reports, 6(1).
Abbey, B. et al., 2016. X-ray laser-induced electron dynamics observed by femtosecond diffraction from nanocrystals of Buckminsterfullerene. Science Advances, 2(9), pp.e1601186-e1601186.
Robinson, P.J. et al., 2016. Structure of a Complete Mediator-RNA Polymerase II Pre-Initiation Complex. Cell, 166(6), pp.1411-1422.e16.
Saldin, D., 2016. Ghost imaging with x rays. Physics, 9.
Calvey, G.D. et al., 2016. Mixing injector enables time-resolved crystallography with high hit rate at X-ray free electron lasers. Structural Dynamics, 3(5), p.054301.
Wu, Y. et al., 2016. The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. Nature Structural & Molecular Biology, 23(10), pp.933-940.
Chang, C.-Y. et al., 2016. Crystal Structures of SgcE6 and SgcC, the Two-Component Monooxygenase That Catalyzes Hydroxylation of a Carrier Protein-Tethered Substrate during the Biosynthesis of the Enediyne Antitumor Antibiotic C-1027 inStreptomyces globisporus. Biochemistry, 55(36), pp.5142-5154.
Spence, J., 2016. Electron Crystallography, Charge-Density Mapping and Nanodiffraction. Transmission Electron Microscopy, pp.145-166.
Zhu, L. et al., 2016. Serial Femtosecond Crystallography of Membrane Proteins. The Next Generation in Membrane Protein Structure Determination, pp.151-160.
Nogly, P. et al., 2016. Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Nature Communications, 7, p.12314.
Rudolf, J.D. et al., 2016. Structure of the ent -Copalyl Diphosphate Synthase PtmT2 from Streptomyces platensis CB00739, a Bacterial Type II Diterpene Synthase . Journal of the American Chemical Society, 138(34), pp.10905-10915.
Mahapatra, M. et al., 2016. Enhanced hydrogenation activity and diastereomeric interactions of methyl pyruvate co-adsorbed with R-1-(1-naphthyl)ethylamine on Pd(111). Nature Communications, 7, p.12380.
Yan, M. et al., 2016. Succinyl-5-aminoimidazole-4-carboxamide-1-ribose 5′-Phosphate (SAICAR) Activates Pyruvate Kinase Isoform M2 (PKM2) in Its Dimeric Form. Biochemistry, 55(33), pp.4731-4736.
Munke, A. et al., 2016. Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source. Scientific Data, 3, p.160064.
Hantke, M.F. et al., 2016. A data set from flash X-ray imaging of carboxysomes. Scientific Data, 3, p.160061.
Ekeberg, T. et al., 2016. Single-shot diffraction data from the Mimivirus particle using an X-ray free-electron laser. Scientific Data, 3, p.160060.
Van der Schot, G. et al., 2016. Open data set of live cyanobacterial cells imaged using an X-ray laser. Scientific Data, 3, p.160058.
White, T.A. et al., 2016. Serial femtosecond crystallography datasets from G protein-coupled receptors. Scientific Data, 3, p.160057.
Lawrence, R.M., Zook, J.D. & Hogue, B.G., 2016. Full inactivation of alphaviruses in single particle and crystallized forms. Journal of Virological Methods, 236, pp.237-244.
Liu, H. & Spence, J.C.H., 2016. XFEL data analysis for structural biology. Quantitative Biology, 4(3), pp.159-176.
He, H. et al., 2016. Improving the efficiency of molecular replacement by utilizing a new iterative transform phasing algorithm. Acta Crystallographica Section A Foundations and Advances, 72(5), pp.539-547.
Huang, T. et al., 2016. Crystal structure of SgcJ, an NTF2-like superfamily protein involved in biosynthesis of the nine-membered enediyne antitumor antibiotic C-1027. The Journal of Antibiotics, 69(10), pp.731-740.
Drozdetski, A.V. et al., 2016. Opposing Effects of Multivalent Ions on the Flexibility of DNA and RNA. Physical Review Letters, 117(2).
Huber, T.D. et al., 2016. Functional AdoMet Isosteres Resistant to Classical AdoMet Degradation Pathways. ACS Chemical Biology, 11(9), pp.2484-2491.
Spence, J. & Lattman, E., 2016. Imaging enzyme kinetics at atomic resolution. IUCrJ, 3(4), pp.228-229.
Dow, X.Y. et al., 2016. Second harmonic generation correlation spectroscopy for characterizing translationally diffusing protein nanocrystals. Acta Crystallographica Section D Structural Biology, 72(7), pp.849-859.
Ranji, M. et al., 2016. Optical Cryoimaging Reveals a Heterogeneous Distribution of Mitochondrial Redox State in ex vivo Guinea Pig Hearts and its Alteration during Ischemia and Reperfusion. IEEE Journal of Translational Engineering in Health and Medicine, pp.1-1.
Nguyen, H.T. et al., 2016. Extracting water and ion distributions from solution x-ray scattering experiments. The Journal of Chemical Physics, 144(21), p.214105.
Yang, M., Nelson, R. & Ros, A., 2016. Toward Analysis of Proteins in Single Cells: A Quantitative Approach Employing Isobaric Tags with MALDI Mass Spectrometry Realized with a Microfluidic Platform. Analytical Chemistry, 88(13), pp.6672-6679.
Pabit, S.A. et al., 2016. Understanding nucleic acid structural changes by comparing wide-angle x-ray scattering (WAXS) experiments to molecular dynamics simulations. The Journal of Chemical Physics, 144(20), p.205102.
Mariani, V. et al., 2016. OnDA: online data analysis and feedback for serial X-ray imaging. Journal of Applied Crystallography, 49(3), pp.1073-1080.
Stan, C.A. et al., 2016. Liquid explosions induced by X-ray laser pulses. Nature Physics, 12(10), pp.966-971.
Berg, J.M. et al., 2016. Preprints for the life sciences. Science, 352(6288), pp.899-901.
Mishin, A.V. et al., 2016. Expression and purification of an engineered human endothelin receptor B in a monomeric form. Doklady Biochemistry and Biophysics, 467(1), pp.157-161.
Nelson, G. et al., 2016. Three-dimensional-printed gas dynamic virtual nozzles for x-ray laser sample delivery. Optics Express, 24(11), p.11515.
Kirian, R.A. & Chapman, H.N., 2016. Imaging of Objects by Coherent Diffraction of X-Ray Free-Electron Laser Pulses. Synchrotron Light Sources and Free-Electron Lasers, pp.1135-1195.
Dörner, K. et al., 2016. Characterization of Protein Nanocrystals Based on the Reversibility of Crystallization. Crystal Growth & Design, 16(7), pp.3838-3845.
Pande, K. et al., 2016. Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein. Science, 352(6286), pp.725-729.
Luo, J. et al., 2016. Deterministic Absolute Negative Mobility for Micro- and Submicrometer Particles Induced in a Microfluidic Device. Analytical Chemistry, 88(11), pp.5920-5927.
Martin-Garcia, J.M. et al., 2016. Serial femtosecond crystallography: A revolution in structural biology. Archives of Biochemistry and Biophysics, 602, pp.32-47.
Hutchison, C.D.M. et al., 2016. Photocycle populations with femtosecond excitation of crystalline photoactive yellow protein. Chemical Physics Letters, 654, pp.63-71.
Cao, H. et al., 2016. Structural dynamics of a methionine Îł-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate. Structural Dynamics, 3(3), p.034702.
Wang, R.Y.-R. et al., 2016. Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta.
Fung, R. et al., 2016. Dynamics from noisy data with extreme timing uncertainty. Nature, 532(7600), pp.471-475.
Stevenson, H.P. et al., 2016. Transmission electron microscopy for the evaluation and optimization of crystal growth. Acta Crystallographica Section D Structural Biology, 72(5), pp.603-615.
Anon, 2016. Correction for Thomaston et al., High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction. Proceedings of the National Academy of Sciences, 113(18), pp.E2548-E2548.
Mavor, D. et al., 2016. Determination of ubiquitin fitness landscapes under different chemical stresses in a classroom setting. eLife, 5.
Tolokh, I.S. et al., 2016. Multi-shell model of ion-induced nucleic acid condensation. The Journal of Chemical Physics, 144(15), p.155101.
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.
Azubel, M. & Kornberg, R.D., 2016. Synthesis of Water-Soluble, Thiolate-Protected Gold Nanoparticles Uniform in Size. Nano Letters, 16(5), pp.3348-3351.
Tokuda, J.M., Pabit, S.A. & Pollack, L., 2016. Protein-DNA and ion-DNA interactions revealed through contrast variation SAXS. Biophysical Reviews, 8(2), pp.139-149.
White, T.A. et al., 2016. Recent developments in CrystFEL . J Appl Crystallogr, 49(2), pp.680-689.
Van Benschoten, A.H. et al., 2016. Measuring and modeling diffuse scattering in protein X-ray crystallography. Proceedings of the National Academy of Sciences, 113(15), pp.4069-4074.
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.
Fuchs, M., 2016. Anomalous Nonlinear X-ray Compton Scattering. High-Brightness Sources and Light-Driven Interactions.
Meyer, P.A. et al., 2016. Data publication with the structural biology data grid supports live analysis. Nature Communications, 7, p.10882.
Barnes, C.O. et al., 2016. Assessment of microcrystal quality by transmission electron microscopy for efficient serial femtosecond crystallography. Archives of Biochemistry and Biophysics, 602, pp.61-68.
Kärtner, F.X. et al., 2016. AXSIS: Exploring the frontiers in attosecond X-ray science, imaging and spectroscopy. Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, 829, pp.24-29.
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.
Uddin, M., 2016. Reconstructing three-dimensional helical structure with an X-ray free electron laser. Journal of Applied Crystallography, 49(2), pp.450-456.
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.
Samuel, P.P. et al., 2016. An in Vitro Investigation of Globin Folding and Expression. Biophysical Journal, 110(3), p.209a-210a.
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. 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.
Sushko, M.L. et al., 2016. The Role of Correlation and Solvation in Ion Interactions with B-DNA. Biophysical Journal, 110(2), pp.315-326.
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.
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.
Sutton, J.L. & Pollack, L., 2015. Tuning RNA Flexibility with Helix Length and Junction Sequence. Biophysical Journal, 109(12), pp.2644-2653.
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.
Heifetz, A. et al., 2016. The Fragment Molecular Orbital Method Reveals New Insight into the Chemical Nature of GPCR-Ligand Interactions. Journal of Chemical Information and Modeling, 56(1), pp.159-172.
Helmich, K.E. et al., 2015. Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-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.
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.
Eagen, K.P., Hartl, T.A. & Kornberg, R.D., 2015. Stable Chromosome Condensation Revealed by Chromosome Conformation Capture. Cell, 163(4), pp.934-946.
Lorch, Y. & Kornberg, R.D., 2015. Chromatin-remodeling and the initiation of transcription. Quarterly Reviews of Biophysics, 48(04), pp.465-470.
Miller, R.L. et al., 2015. The Importance of Ligand-Receptor Conformational Pairs in Stabilization: Spotlight on the N/OFQ G Protein-Coupled Receptor. Structure, 23(12), pp.2291-2299.
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.
Bogorodskiy, A. et al., 2015. Nucleation and Growth of Membrane Protein CrystalsIn Meso--A Fluorescence Microscopy Study. Crystal Growth & Design, 15(12), pp.5656-5660.
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