BioSAXS-2000ⁿᵃⁿᵒ

BioSAXS-2000ⁿᵃⁿᵒ
Kratky SAXS for proteins and macromolecules Kratky SAXS for proteins and macromolecules Kratky SAXS for proteins and macromolecules
Características
  • Un sistema SAXS compacto que ofrece datos de alta calidad para una amplia gama de muestras.
  • Sistema totalmente automático de medición y análisis de datos para diversas muestras.
  • Alta resolución angular con opción para la recolección de datos WAXS.
  • Captadores de haz primario de fotodiodo para mediciones de intensidad y corrección de absorción de muestra.
  • Control de la temperatura de la muestra incluido con el sistema.
  • Software de recopilación y procesamiento de datos SAXSLab.

Sistema de cámara Kratky de dispersión de rayos X por ángulo pequeño (SAXS)

Dispersión de macromoléculas por ángulo pequeño

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Features | Specifications | Video | Accessories | Applications | Publications
 

La cámara BioSAXS-2000nano SAXS de Rigaku está diseñada específicamente para satisfacer las necesidades del biólogo estructural. Basado en un diseño patentado bidimensional de Kratky, el BioSAXS-2000nano ocupa mucho menos espacio que una cámara convencional de 3 pinholes (orificios), pero ofrece mejores características de flujo. Lo mejor de todo es que el BioSAXS-2000nano se puede montar en el puerto abierto de un generador de rayos X de ánodo giratorio de Rigaku, aprovechando al máximo la infraestructura existente, o se puede acoplar a una fuente de rayos X con microfoco de tubo sellado de Rigaku. La configuración BioSAXS AUTO incorpora dos características que ahorran tiempo: un Cambiador Automático de Muestras para la operación desatendida durante la noche y un Análisis Automático de Procesos basada en el paquete estándar mundial ATSAS de EMBL Hamburg.

No es necesario esperar por la línea de haz en un sincrotrón

El BioSAXS-2000nano está equipado con la nueva óptica OptiSAXS, una óptica multicapa de doble enfoque cuyo foco está en el detector. En comparación con su predecesor, OptiSAXS proporciona una mejora de doble flujo, lo que resulta en un mayor brillo en la posición de la muestra y una recolección de datos en el rango de minutos. Por lo tanto, el BioSAXS-2000nano brinda una experiencia de línea de haz a los experimentos SAXS de laboratorios caseros.

Accesorios opcionales

  • Cambiador automático de muestras (ASC) con soporte para hasta 96 muestras
  • Análisis Automático de Proceso (AAP) basado en ATSAS; el software de análisis SAXS más popular del mundo, desarrollado en EMBL Hamburg
Specifications
Varía según la configuración ">
Nombre del producto BioSAXS-2000nano
Técnica Dispersión biológica por ángulo pequeño
Ventajas Cámara SAXS para laboratorio casero
Tecnología SAXS Kratky bidimensionales
Atributos principales Diseño compacto, óptica OptiSAXS, colimación Kratky 2D
Opciones principales Cambiador automático de muestras
Análisis Automático de Proceso (AAP) basado en ATSAS

 
Computadora PC externa, sistema operativo MS Windows®
Dimensiones principales
Cuerpo Varía según la configuración
Requerimientos de energía Varía según la configuración

 

BioSAXS publications

  • Esteban Florez LE, Trofimov AA, Ievlev A, Qian s, Rondinone AJ, Khajotia SS. “Advanced characterization of surface-modified nanoparticles and nanofilled antibacterial dental adhesive resins.” (2020) Sci Rep 10, 9811. https://doi.org/10.1038/s41598-020-66819-8
  • Doktorova M, Kučerka N, Kinnun JJ, Pan J, Marquardt D, Scott HL, Venable RM, Pastor RW, Wassall SR, KatsarasJ, Heberle FA. “Molecular Structure of Sphingomyelin in Fluid Phase Bilayers Determined by the Joint Analysis of Small-Angle Neutron and X-ray Scattering Data.” (2020) The Journal of Physical Chemistry B 124 (25), 5186-5200. https://doi.org/10.1021/acs.jpcb.0c03389
  • Nakamura T, Hashikawa C, Okabe K, Yokote Y, Chirifu M, Toma-Fukai S, Nakamura N, Matsuo M, Kamikariya M, Okamoto Y, Gohda J, Akiyama T, Semba K, Ikemizu S, Otsuka M, Inoue J, Yamagata Y. “Structural analysis of TIFA: Insight into TIFA-dependent signal transduction in innate immunity.” (2020) Sci Rep 10, 5152. https://doi.org/10.1038/s41598-020-61972-6
  • Johansson E, Nielsen AD, Demuth H, Wiberg C, Schjødt CB, Huang T, Chen J, Jensen S, Petersen J, Thygesen P. “Identification of Binding Sites on Human Serum Albumin for Somapacitan, a Long-Acting Growth Hormone Derivative.” (2020) Biochemistry 59 (14), 1410-1419. https://doi.org/10.1021/acs.biochem.0c00019
  • Vykoukal V, Zelenka F, Bursik J, Kana T, Kroupa A, Pinkas J. “Thermal properties of Ag@Ni core-shell nanoparticles.” (2020) Calphad 69: 101741. https://doi.org/10.1016/j.calphad.2020.101741
  • Heberle FA, Doktorova M, Scott HL, Skinkle A, Waxham MN, Levental I. “Direct label-free imaging of nanodomains in biomimetic and biological membranes by cryogenic electron microscopy.” (2020). https://doi.org/10.1101/2020.02.05.935551
  • Sherekar M, Han S, Ghirlando R, Messing S, Drew M, Rabara D, Waybright T, Juneja P, O'Neill H, Stanley CB, Bhowmik D, Ramanathan A, Subramaniam S, Nissley DV, Gillette W, McCormick F, Esposito D. “Biochemical and structural analyses reveal that the tumor suppressor neurofibromin (NF1) forms a high-affinity dimer.” (2020) J. Biol. Chem. 295: 1105-1119. https://doi.org/10.1074/jbc.RA119.010934.
  • DiPasquale M, Nguyen MHL, Rickeard BW, Cesca N, Tannous C, Castillo SR, Katsaras J, Kelley EG, Heberle FA, Marquardt D. “The antioxidant vitamin E as a membrane raft modulator: Tocopherols do not abolish lipid domains.” (2020) Biochimica et Biophysica Acta (BBA) – Biomembranes 1862 (8) 183189. https://doi.org/10.1016/j.bbamem.2020.183189
  • White MA, Tsalkova T, Mei FC, Cheng X. “Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology.” (2020) Cells 9(1), 35. https://doi.org/10.3390/cells9010035

  • Bishnoi R, Sousa GL, Contet A, Day CJ, Hou CD, Profitt LA, Singla D, Jennings MP, Valentine AM, Povelones M, Baxter RHG. “Solution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2.” (2019) bioRxiv 565705. https://doi.org/10.1101/565705
  • Luo Z, Murello A, Wilkins DM, Kovacik F, Kohlbrecher J, Radulescu A, Okur HI, Ong QK, Roke S, Ceriotti M, Stellacci F. “Determination and evaluation of the nonadditivity in wetting of molecularly heterogeneous surfaces.” (2019) Proceedings of the National Academy of Sciences 116 (51) 25516-25523. https://doi.org/10.1073/pnas.1916180116
  • Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G. “Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii.” (2019) J. Biol. Chem. 295: 170-. https://doi.org/10.1074/jbc.RA119.008735
  • Vykoukal V, Halasta V, Babiak M, Bursik J, Pinkas J. “Morphology Control in AgCu Nanoalloy Synthesis by Molecular Cu(I) Precursors.” (2019) Inorg. Chem. 58 (22) 15246–15254. https://doi.org/10.1021/acs.inorgchem.9b02172.
  • Matsumoto T, Yamano A, Murakawa Y, Fukada H, Sawa M, Kinoshita T. “Ensemble structural analyses depict the regulatory mechanism of non-phosphorylated human MAP2K4.” (2019) Biochemical and Biophysical Research Communications 521 (1) 106-112. https://doi.org/10.1016/j.bbrc.2019.10.086
  • Cho HS, Lee Y, Wu J, Shin SR, Kang JK, Terasaki O. “Understanding Adsorption Behavior of Periodic Mesoporous Organosilica Having a Heterogeneous Chemical Environment: Selective Coverage and Interpenetration of Adsorbates inside the Channel Wall.” (2019) The Journal of Physical Chemistry C 123 (40) 24884-24889. https://doi.org/10.1021/acs.jpcc.9b06523
  • Shrestha UR, Juneja P, Zhang Q, Gurumoorthy V, Borreguero JM, Urban V, Cheng X, Pingali SV, Smith JC, O’Neill HM, Petridis L. "Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation." (2019) Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1907251116
  • Nanji T, Gehrke EJ, Shen Y, Gloyd M, Zhang X, Firby CD, Huynh A, Razi A, Ortega J, Elliot MA, Guarné A. "Streptomyces IHF uses multiple interfaces to bind DNA." (2019) Biochimica et Biophysica Acta (BBA) - General Subjects 1863, 129405. https://doi.org/10.1016/j.bbagen.2019.07.014
  • Fioravanti A, Hauwermeiren FV, Verren SEV der, Jonckheere W, Goncalves A, Pardon E, Steyaert J, Greve HD, Lamkanfi M, Remaut H. "Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax." (2019) Nat Microbiol 1–10. https://doi.org/10.1038/s41564-019-0499-1
  • Wang L, Suganuma S, Hibino A, Mitsui R, Tani A, Matsumoto T, Ebihara A, Fitriyanto NA, Pertiwiningrum A, Shimada M, Hayakawa T, Nakagawa T. "Lanthanide-dependent methanol dehydrogenase from the legume symbiotic nitrogen-fixing bacterium Bradyrhizobium diazoefficiens strain USDA110." (2019) Enzyme and Microbial Technology 130, 109371. https://doi.org/10.1016/j.enzmictec.2019.109371
  • Pawar AD, Kiran U, Raman R, Chandani S, Sharma Y. "Abundant Perithecial Protein (APP) from Neurospora is a primitive functional analog of ocular crystallins." (2019) Biochemical and Biophysical Research Communications 516, 796–800. https://doi.org/10.1016/j.bbrc.2019.06.102
  • Abe H, Takekiyo T, Yoshimura Y, Shimizu A. "Static and dynamic properties of nano-confined water in room-temperature ionic liquids." (2019) Journal of Molecular Liquids 290, 111216. https://doi.org/10.1016/j.molliq.2019.111216
  • White MR, Mitrea DM, Zhang P, Stanley CB, Cassidy DE, Nourse A, Phillips AH, Tolbert M, Taylor JP, Kriwacki RW. "C9orf72 Poly(PR) Dipeptide Repeats Disturb Biomolecular Phase Separation and Disrupt Nucleolar Function." (2019) Molecular Cell: In Press, Corrected Proof, Available online 10 April 2019. https://doi.org/10.1016/j.molcel.2019.03.019
  • Bishnoi R, Contet A, Day CJ, Hou DC, Profitt LA, Singla D, Sousa GL, Jennings MP, Povelones M, Valentine VM, Baxter RHG. "C- type lectins CTL4 and CTLMA2: conserved heterodimeric structure and glycan specificity in Anopheles mosquitoes." (2019) bioRxiv 565705; doi: https://doi.org/10.1101/565705
  • Mok MCY, Campalans A, Pillon MC, Guarné A, Radicella JP, Junop MS. "Identification of an XRCC1 DNA binding activity essential for retention at sites of DNA damage." (2019) Scientific Reportsvolume 9:3095. https://doi.org/10.1038/s41598-019-39543-1
  • Jia T, Wang Y, Dou Y, Li Y, Jung de Andrade M, Wang R, Fang S, Li J, Yu Z, Qiao R, Liu Z. "Moisture Sensitive Smart Yarns and Textiles from Self‐Balanced Silk Fiber Muscles." (2019) Advanced Functional Materials. 2019:1808241. https://doi.org/10.1002/adfm.201808241
  • Kildegaard J, Buckley ST, Nielsen RH, Povlsen GK, Seested T, Ribel U, Olsen HB, Ludvigsen S, Jeppesen CB, Refsgaard HHF, Bendtsen KM, Kristensen NR, Hostrup S, Sturis J. "Elucidating the Mechanism of Absorption of Fast-Acting Insulin Aspart: The Role of Niacinamide." (2019) Pharm Res 36: 49. https://doi.org/10.1007/s11095-019-2578-7
  • Nandwani N, Surana P, Negi H, Mascarenhas N, Udgaonkar J, Das R, Gosavi S. "A five-residue motif for the design of domain swapping in proteins." (2019) Nature Communications 10:452, https://doi.org/10.1038/s41467-019-08295-x

  • Brady NG, Qian S, Bruce BD. "Analysis of Styrene Maleic Acid Alternating Copolymer Supramolecular Assemblies in Solution by Small Angle X-Ray Scattering." (2018) Eur Polymer J Pub Date : 2018-11-20, https://doi.org/10.1016/j.eurpolymj.2018.11.0344
  • Kooshapur H, Choudhury NR, Simon B, Mühlbauer M, Jussupow A, Fernandez N, Jones AN, Dallmann A, Gabel F, Camilloni C, Michlewski G, Caceres JF, Sattler M. "Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP." (2018) Nature Communications 9:2479. https://doi.org/10.1038/s41467-018-04871-9
  • Moonens K, Hamway Y, Neddermann M, Reschke M, Tegtmeyer N, Kruse T, Kammerer R, Mejías‐Luque R, Singer BB, Backert S, Gerhard M, Remaut H. "Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs." (2018) EMBO Journal Jun 1. pii: e98665. https://doi.org/10.15252/embj.201798665
  • Vykoukal V, Bursik J, Roupcova P, Cullen DA, Pinkas J. "Solvothermal hot injection synthesis of core-shell AgNi nanoparticles." J Alloys & Compounds (2018) 770:377-385. https://doi.org/10.1016/j.jallcom.2018.08.082
  • Frampton MB, Nguyen MHL, DiPasquale M, Dick R, Marquardt D, Zelisko PM. "Characterization of self-assembled hybrid siloxane-phosphocholine bilayers." Chemistry & Physics of Lipids (2018) 216:1-8 https://doi.org/10.1016/j.chemphyslip.2018.07.007
  • Liu J, Misra A, Reddy S, White MA, Ren G, Rudenko G. "Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer." (2018) JMB 430 (21):4325-4343. https://doi.org/10.1016/j.jmb.2018.08.026
  • Harsini FM, Chebrolu s, fuson KL, White MA, Rice AM, Sutton RB. "FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins." Scientific Reports (2018) 8:10949 https://doi.org/10.1038/s41598-018-29184-1
  • Srivastava SS, Raman R, Kiran U, Garg R, Chadalawada S, Pawar AD, Sankaranarayanan R, Sharma Y. "Interface interactions between βγ‐crystallin domain and Ig‐like domain render Ca2+‐binding site inoperative in abundant perithecial protein of Neurospora crassa." Mol Microbiology (2018) 110(6):955-972. https://doi.org/10.1111/mmi.14130
  • Suárez IP, Gauto DF, Hails G, Mascali FC, Crespo R, Zhao L, Wang J, RasiaRM. "Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1." Phys. Chem. Chem. Phys., 2018,20, 11237-11246. https://doi.org/10.1039/C7CP07908G
  • Will N, Lee K, Hajredini F, Giles DH, Abzalimov RR, Clarkson M, Dalby KN, Ghose R. "Structural Dynamics of the Activation of Elongation Factor 2 Kinase by Ca2+-Calmodulin." J Mol Biol. 2018 May 22. pii: S0022-2836(18)30486-8. https://doi.org/10.1016/j.jmb.2018.05.033.
  • Kawada Y, Goshima T, Sawamura R, Yokoyama S, Yanase E, Niwa T, Ebihara A, Inagaki M, Yamaguchi K, Kuwata K, Kato Y, Sakurada O, Suzuki T. "Daidzein reductase of Eggerthella sp. YY7918, its octameric subunit structure containing FMN/FAD/4Fe-4S, and its enantioselective production of R-dihydroisoflavones." (2018) J. Biosci & Bioeng: Available online 23 April 2018. https://doi.org/10.1016/j.jbiosc.2018.03.018
  • Suárez IP, Gauto DF, Hails G, Mascali FC, Crespo R, Zhao L, Wang J, Rasia RM. "Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1." (2018) Phys. Chem. Chem. Phys., 20, 11237-11246. http://dx.doi.org/10.1039/C7CP07908G
  • Mitrea DM, Cika JA, Stanley CB, Nourse A, Onuchic PL, Banerjee PR, Phillips AH, Park C-G, Deniz AA, Kriwacki RW. "Self-interaction of NPM1 modulates multiple mechanisms of liquid–liquid phase separation." (2018) Nature Communications 9: 842. https://doi.org/10.1038/s41467-018-03255-3.
  • Marquardt D, Frontzek MD, Zhao Y, Chakoumakos BC, Katsaras J. "Neutron diffraction from aligned stacks of lipid bilayers using the WAND instrument." (2018) J. Appl. Cryst. 51: (2). https://doi.org/10.1107/S1600576718001243
  • Yoshida H, Park S-Y, Oda T, Akiyoshi T, Sato M, Shirouzu M, Tsuda K, Kuwasko K, Unzai S, Muto Y, Urano T, Obayashi E. "A novel 3' splice site recognition by the two zing fingers in the U2AF small subunit." (2018) Genes & Dev. 29: 1649-1660.
  • Nakashima R, Sakurai K, Yamaguchi A. "Crystallographic Analysis of Drug and Inhibitor-Binding Structure of RND-Type Multidrug Exporter AcrB in Physiologically Relevant Asymmetric Crystals." (2018) In: Yamaguchi A., Nishino K. (eds) Bacterial Multidrug Exporters. Methods in Molecular Biology, vol 1700. Humana Press, New York, NY.

  • Eisemann T. Structural Analysis of Tankyrase-1 Regulation and Binding Partner Interaction. (2017). (Doctoral dissertation, Thomas Jefferson University).
  • Jasnovidova O, Klumpler T, Kubicek K, Kalynych S, Plevka P, Stefl R. "Structure and dynamics of the RNAPII CTDsome with Rtt103." PNAS (2017) 114 (42): 11133-11138. https://doi.org/10.1073/pnas.1712450114.
  • Nečasová I, Janoušková E, Klumpler T, Hofr C. "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it." Nucleic Acids Res (2017) https://doi.org/10.1093/nar/gkx812.
  • Vandervelde A, Drobnak I, Hadži S, Sterckx YG-J, Welte T, De Greve H, Charlier D, Efremov R, Loris R, Lah J. "Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon." Nucleic Acids Res (2017) doi: 10.1093/nar/gkx108.
  • Sankhala RS, Lokareddy RK, Begum S, Pumroy RA, Gillilan RE, Cingolani G. “Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.” Nature Comm (2017) 8:979 doi: 10.1038/s41467-017-01057-7.
  • Singh RK, Steyaert J, Versees W. "Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis." Protein Science. doi:10.1002/pro.3141.
  • Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W. “Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence.” JBC (2017) 292, 5871-5883. doi: 10.1074/jbc.M116.761809.
  • Niwa S, Nakamura F, Tomabechi Y, Aoki M, Shigematsu H, Matsumoto T, Yamagata A, Fukai S, Hirokawa N, Goshima Y, Shirouzu M, Nitta R. "Structural basis for CRMP2-induced axonal microtubule formation." Scientific Reports (2017) 7: 10681. http://doi.org/10.1038/s41598-017-11031-4
  • Szymanski MR, Yu W, Gmyrek AM, White MA, Molineux IJ, Lee JC, Yin YW. "A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease." Nature Comm (2017) 8:14959 doi: 10.1038/ncomms1495.
  • Suzukia T, Sagane Y, Matsumoto T, Hasegawa K, Yamano A, Niwa K, Watanabe T. "Building-block architecture of botulinum toxin complex: Conformational changes provide insights into the hemagglutination ability of the complex" Biochemistry and Biophysics Reports, Volume 9, March 2017, Pages 67–71.
  • Grushin K, White MA, Stoilova-McPhie S. "Reversible stacking of lipid nanodiscs for structural studies of clotting factors." Nanotechnology Reviews (2017) 6 (1):139-148. https://doi.org/10.1515/ntrev-2016-0073.
  • Guan H, Tian J, Qin B, Wojdyla JA, Wang B, Zhao Z, Wang M, Cui S. "Crystal structure of 2C helicase from enterovirus 71." Science Advances (2017) 3 (4): e1602573, DOI: 10.1126/sciadv.1602573.
  • Jo CH, Son J, Kim S, Oda T, Kim J, Lee M, Sato M, Kim HT, Unzai S, Park S, Hwang KY. "Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis." Scientific Reports. (2017) 7:1764. doi:10.1038/s41598-017-02044-0.
  • Kooshapur H, Choudhury NR, Simon B, Muehlbauer M, Jussupow A, Fernandez N, Dallmann A, Gabel F, Camilloni C, Michlewski G, Caceres JF, Sattler M. "Structural basis for terminal loop recognition and processing of pri-miRNA-18a by hnRNP A1." bioRxiv (2017) doi: https://doi.org/10.1101/178855.
  • Lu C, Chiang W, Du H, Li J, Gan L. Zhang X, Chu X, Yao Y, Li B, Kang F. “Thermal conductivity of electrospinning chain-aligned polyethylene oxide (PEO).” Polymer (2017) 115 (21): 52-59.
  • Takekiyo T, Yoshimura Y. "Ionic Liquid-Induced Unique Structural Transitions of Proteins." Progress and Developments in Ionic Liquids, Prof. Scott Handy (Ed.), InTech, DOI: 10.5772/65886. Available from: https://www.intechopen.com/books/progress-and-developments-in-ionic-liquids/ionic-liquid-induced-unique-structural-transitions-of-proteins.
  • Marquardt D, Heberle FA, Miti T, Eicher B, London E, Katsaras J, Pabst G. "1H NMR Shows Slow Phospholipid Flip-Flop in Gel and Fluid Bilayers." Langmuir (2017) 33 (15): 373-3741 doi:10.1021/acs.langmuir.6b04485.

  • Eisemann T, McCauley M, Langelier M, Gupta K, Roy S, Van Duyne GD, Pascal JM. "Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification." Structure (2016) 24, 1679–1692 https://doi.org/10.1016/j.str.2016.07.014
  • Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N. "Structure of the NPr:EINNtr Complex: mechanism for specificity in paralogous phosphotransferase systems." Structure (2016) 24 (12): 2127–2137.
  • Cura V, Marechal N, Troffer-Charlier N, Strub JM, van Haren MJ, Martin NI, Cianférani S, Bonnefond Luc, Cavarelli J. "Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors." The FEBS Journal. doi: 10.1111/febs.13953.
  • Suzuki T, Sagane Y, Matsumoto T, Hasegawa K, Yamano A, Niwa K, Watanabe T. "Building-block architecture of botulinum toxin complex: conformational changes provide insights into the hemagglutination ability of the complex." Biochem and Biophys Reports. (2016) doi: http://dx.doi.org/10.1016/j.bbrep.2016.11.008.
  • Jia D, Zhang J, Li F, Wang J, Deng Z, White MA, Osborne DG, Phillips-Krawczak C, Gomez TS, Li H, Singla A, Burstein E, Billadeau DD, Rosen MK. "Structural and mechanistic insights into regulation of the rotamer coat by TBC1d5." Nature Comm (2016) 7:13305 doi:10.1038/ncomms13305
  • Inouye H, Houde D, Temel DB, Makowski L. "Utility of Solution X-ray Scattering for the Development of Antibody Biopharmaceuticals." J Pharma Sci. (2016) doi: http://dx.doi.org/10.1016/j.xphs.2016.07.021.
  • Miyashita S, Sagane Y, Suzuki T, Matsumoto T, Niwa K, Watanabe T. "Non-Toxic Proteins of the Botulinum Toxin Complex Exert In-vivo Toxicity." Scientific Reports (2016) 6:31043, doi: 10.1038/srep31043.
  • Wan LCK, Pillon MC, Thevakumaran N, Sun Y, Chakrabartty A, Guarné A, Kurinov I, Durocher D, Sicheri F. "Structural and functional characterization of KEOPS dimerization by Pcc1 and its role in t6A biosynthesis." Nucleic Acids Res. (2016) doi: 10.1093/nar/gkw542
  • Zorzini V, Mernik A, Lah J, Sterckx YGJ, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. "Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF." J Biol Chem (2016) 291, 10950-10960.
  • Goricanec D, Stehle R, Egloff P, Grigoriu S, Plückthun A, Wagner G, Hagn F. "Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding." PNAS (2016) 113 (26) E3629-E3638. doi: 10.1073/pnas.1604125113.
  • Stogios PJ, Cox G, Spanogiannopoulos P, Pillon MC, Waglechner N, Skarina T, Koteva K, Guarné A, Savchenko A, Wright GD. "Rifampin phosphotransferase is an unusual antibiotic resistance kinase." Nature Communications 7, Article number: 11343. doi: 10.1038/ncomms1134
  • Skoda D, Styskalik A, Moravec Z, Bezdicka P, Babiak M, Klementova M, Barnes CE, Pinkas J. "Novel non-hydrolytic templated sol–gel synthesis of mesoporous aluminosilicates and their use as aminolysis catalysts." RSC Adv. (2016), 6, 24273–84. doi: 10.1039/C5RA24563J.
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