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Kleinwinkelröntgenstreuung (SAXS) Kratky Kamerasystem

Strukturbestimmung von Proteinen

Die BioSAXS-2000 SAXS Kamera von Rigaku wurde speziell für die Anforderungen von Strukturbiologen entwickelt. Auf der Basis des patentierten, zweidimensionalen Kratky-Designs besitzt das BioSAXS-2000 einen geringeren Platzbedarf im Vergleich zur konventionellen 3-Lochkamera, bietet jedoch bessere Fluxcharakteristika. Der größte Vorteil jedoch liegt darin, dass das BioSAXS-2000 auf den offenen Port des Drehanoden-Röntgengenerators von Rigaku montiert werden kann. Die bestehende Ausstattung kann so voll genutzt werden. Zusätzlich kann das BioSAXS-2000 mit einer versiegelten Mikrofokus-Röntgenröhre von Rigaku gekoppelt werden. Die AUTO-Konfiguration des BioSAXS berücksichtigt dabei zwei zeitsparende Eigenschaften: einen automatischen Probenwechsler für den unbeaufsichtigten Betrieb über Nacht sowie eine automatische Analysen-Pipeline auf der Basis des weltweit gültigen Standards des ATSAS Pakets von EMBL (Hamburg).

Kein Grund auf Synchrotron-Messzeiten warten zu müssen

Das BioSAXS-2000 ist mit der neuen OptiSAXS Optik ausgestattet, einem optischen System mit Doppelfokus-Mehrschicht-Technologie und Detektor-Fokus. Im Vergleich zu seinem Vorgänger verbessert das OptiSAXS den Flux um mehr als das Doppelte, was zu höherer Punkthelle in Probenposition und schnellerer Datensammlung im Minutentakt führt. Somit liefert das BioSAXS-2000 Messergebnisse aus SAXS Experimenten in Kleinlaboratorien, die so bisher sonst nur von fortschrittlichen Synchrotrons erzielt werden konnten.

Sonderzubehör

  • Automatischer Probenwechsler (ASC) für 8 bis 96 Proben. Siehe hierzu [Zubehör] für ausführlichere Details.
  • Automatische Analysen-Pipeline (AAP) auf der Basis von ATSAS, der weltweit beliebtesten SAXS-Analyse-Software, entwickelt von EMBL (Hamburg). Siehe hierzu [Zubehör] für ausführlichere Details.

Features

  • Automatische Probenbühne mit drei Kapillarzellen und einer Standardposition für Pulver.
  • Simultane SAXS und WAXS Messungen (qmax = 0.65 Å⁻¹).
  • Einfache Installation mittels verfügbarem Generatoranschluss. Kann wahlweise auch an eine Röntgenquelle angeschlossen werden: Versiegelte Mikrofokus-Röntgenröhre, MicroMax-007 HF, FR-X.
  • Punktfokus-Optik verhindert mögliche Präzisionsprobleme in Verbindung mit traditionellen Kratky-Kameras.
  • Alle Systemkomponenten k&oml;nnen vom Steuerrechner betrieben werden.
  • Photodioden-Beamstop für Intensitätsmessungen und Probenabsorptionskorrigierung.
  • System mit Proben-Temperaturkontrolle.
  • 2D Kratky-Kollimation berücksichtigt Messungen niedriger q-Werte auch ohne Systemneuausrichtung.
  • SAXSLab Datensammlung und Verarbeitungssoftware.

Below are the specifications for the BioSAXSnano protein small angle scattering X-ray system from Rigaku.


  • Incident Beam: OptiSAXS CMF focusing optic
  • Collimation: 2D Kratky (X stage and tilt, motorized)
  • Beam size at Sample: Variable Width x 1.5 mm²
  • Sample Stage: 3 capillaries (X, Y stage, motorized) with a flow cell option
  • Sample Volume: 20 – 30 μL
  • Sample Temperature Control
  • Beam Stop: PIN diode detector (motorized)
  • q-range: 0.006 Å⁻¹ - 0.6 Å⁻¹
  • Detector: Rigaku HyPix-3000 Hybrid Pixel Array Detector (pixel size: 100 μm, active area: 77.5 mm X 30.5 mm)

Because data collection is faster with the BioSAXS-2000, automated tools for sample mounting, data collection and data analysis become especially important. The BioSAXS AUTO package accomplishes each of those tasks with the Automated Sample Changer (ASC) for automatic sample loading and data collection, and the Automated Analysis Pipeline (AAP) for automatic data processing and analysis.

Description
Automatische Daten-Analysenpipeline

Das AAP nutzt den Industriestandard des ATSAS Pakets um folgende automatisierte Analysen für jede Analysee zu ermöglichen:

  • Automatische Probenauswertung und Identifikation des Aggregationsverhaltens
  • Automatische Mittelwertbildung des Tiefeprofils und Puffersubtraktion
  • Automatische Erstellung von Guinier-Funktionen und Berechnung von Rg and I(0)
  • Automatische Erstellung von Kratky-Funktionen
  • Automatische Berechnung von Porod-Volumen und Molekulargewicht (MW)
  • Automatische Berechnung von P(r) mit Berichterstattung von Rg und Dmax im Realraum
  • Automatische Hüllkurvenberechnung, Mittelwertberechnung und Analyse
  • PDF-Fertigungsberichtgenerator und einfache Übersicht vorangegangener AAP Durchläufe
Das AAP erlaubt rasche Auswertungen der Probenqualität, mit Wiedergabe farbkodierter Ergebnisse. Die Identifizierung und Abgrenzung von Proben mit günstigem Analyseverhalten gegenüber solchen mit negativem Aggregations- oder Konzentrationsverhalten kann somit einfach und rasch vonstatten gehen. 		Automatische Daten-Analysenpipeline
Automatische Probenhandhabung

Das ASC bietet wartungsfreie Probenaufbringung und Datensammlungen für Laboratorien, die besonderen Wert auf eine höhere Durchsatzleistungsfähigkeit des BioSAXS-2000 legen. Das ASC unterstützt dabei die Probenaufbringung mittels 96-Positionshalterung oder 0.2 ml PCR Röhrchenhalterung, wobei ein nahtloser Übergang von Hardware und dem SAXSLab-Software-Paket gewährleist wird.
Probenlösungen können folienversiegelt werden um ein Verdunsten des Lösungsmittels vor der Datensammlung zu verhindern. Das ASC unterstützt darüberhinaus eine temperaturfgeführte Pobenlagerung, mehrere Reinigungsprozesse und Reinigungsprotokolle.

 Automatische Probenhandhabung

Together, the ASC and AAP components of the BioSAXS AUTO package allow unattended sample mounting, data collection and processing to give you a more beamline-like experience, and to allow you to focus more time where it counts: SAXS data analysis and publication of results.

2018

  • 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.

2017

  • 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-liqu....
  • 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.

2016

  • 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.
  • Li Q, Mu Z, Zhao R, Dahal G, Viola RE, Liu T, Jin Q, Cu S. "Structural Insights into the Tetrameric State of Aspartate-β-semialdehyde Dehydrogenases from Fungal Species." Scientific Reports 6, Article number: 21067 (2016) doi:10.1038/srep21067.

2015

  • Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K. "Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis." J. Biol. Chem. (2015) doi: 10.1074/jbc.M115.680934, First published online: October 15, 2015.
  • Pillon MC, Babu VMP, Randall JR, Cai J, Simmons LA, Sutton MD, Guarné A. "The sliding clamp tethers the endonuclease domain of MutL to DNA." Nucl. Acids Res. (2015) doi: 10.1093/nar/gkv918, First published online: September 17, 2015.
  • Zeqiraj E, Tian L, Piggott CA, Pillon MC, Duffy NM, Ceccarelli DF, Keszei AF, Lorenzen K, Kurinov I, Orlicky S, Gish GD, Heck AJ, Guarné A, Greenberg RA, Sicheri F. "Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function." Mol Cell. 2015 Sep 17;59(6):970-83. doi: 10.1016/j.molcel.2015.07.028. Epub 2015 Sep 3.
  • Abe H, Takekiyo T, Aono M, Kishimura H, Yoshimura Y, Hamaya N. "Polymorphs in room-temperature ionic liquids: Hierarchical structure, confined water and pressure-induced frustration." Journal of Molecular Liquids, online proof available 19 June 2015, doi:10.1016/j.molliq.2015.05.057.
  • Zebret S, Vögele E, Klumpler T and Hamacek J. "Designing artificial 3D helicates: unprecedented self-assembly of homo-octauclear tetrapods with Europium." Chemistry. 2015 Apr 27;21(18):6695-9.
  • Aria T, Kimata S, Mochizuki D, Hara K, Zako T, Odaka M, Yohda M, Arisaka F, Kanamaru S, Matsumoto T, Yajima S, Sato J, Kawasaki S, Niimura Y. "NADH oxidase and alkyl hydroperoxide reductase subunit C (peroxiredoxin) from Amphibacillus xylanus form an oligomeric assembly." FEBS Open Bio. 2015, 5:124-131
  • Soh YM, Bürmann F, Shin HC, Oda T, Jin KS, Toseland CP, Kim C, Lee H, Kim SJ, Kong MS, Durand-Diebold ML, Kim YG, Kim HM, Lee NK, Sato M, Oh BH, Gruber S. "Molecular basis for SMC rod formation and its dissolution upon DNA binding." Mol Cell. 2015 Jan 22;57(2):290-303
  • Watanabe-Matsui M, Matsumoto T,Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. "Heme binds to an intrinsically disordered region of Bach2 and alters its conformation." Arch Biochem Biophys. 2015 Jan 1. 565: 25-31
  • Skoda D, Styskalik A, Moravec Z, Bezdicka P, Pinkas J. "Templated non-hydrolytic synthesis of mesoporous zirconium silicates and their catalytic properties." J Mater Sci. 2015, 1-12
  • Criswell A, Mooers BH. "Structural Studies of a Double-Stranded RNA from Trypanosome RNA Editing by Small-Angle X-ray Scattering." Methods Mol Biol. (2015)1240:165-89
  • Sopoušek J, Zobač O, Buršík J, Roupcová P, Vykoukal V, Brož P, Pinkasab J, Vřešt'ál J. "Heat-induced spinodal decomposition of Ag–Cu nanoparticles." Phys Chem Chem Phys, (2015) 17:28277-28285, doi: 10.1039/C5CP00198F.

2014

  • Asencio-Hernández J, Ruhlmann C, McEwen A, Eberling P, Nominé Y, Céraline J, Starck JP, Delsuc MA. "Reversible Amyloid Fiber Formation in the N Terminus of Androgen Receptor." Chembiochem. 2014 Sep 11. doi: 10.1002/cbic.201402420. [Epub ahead of print]
  • Cura V, Troffer-Charlier N, Wurtz JM, Bonnefond L, Cavarelli J. “Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site.” Acta Cryst. (2014). D70, 2401-2412
  • Sopoušek J, Pinkas J, Brož P, Buršík K, Vykoukal V, Škoda D, Stýskalík A, ZobaI O, Vrešt’ál J, Hrdlička A, Šimbera J. “Ag-Cu Colloid Synthesis: Bimetallic Nanoparticle Characterisation and Thermal Treatment.” Journal Nanomaterials, Volume 2014, Article ID 638964, 13 pages
  • Zorba A, Buosi V, Kutter S, Kern N, Pontiggia F, Cho YJ, Kern D. “Molecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2.” Elife. 2014 May 27;3:e02667
  • Sedláček V, Klumpler T, Marek J, Kučera I. “The structural and functional basis of catalysis mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans.” PLoS One. 2014 May 9;9(5):e96262
  • Abe H, Takekiyo T, Shigemi M, Yoshimura Y, Tsuge S, Hanasaki T, Ohishi K, Takata S, Suzuki J. “Direct Evidence of Confined Water in Room-Temperature Ionic Liquids by Complementary Use of Small-Angle X-ray and Neutron Scattering.” J Phys Chem Lett, 2014, 5(7): 1175-1180
  • Huang H, Zeqiraj E, Dong B, Jha BK, Duffy NM, Orlicky S, Thevakumaran N, Talukdar M, Pillon MC, Ceccarelli DF, Wan LC, Juang YC, Mao DY, Gaughan C, Brinton MA, Perelygin AA, Kourinov I, Guarné A, Silverman RH, Sicheri F. "Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity." Mol Cell. 2014 Jan 23;53(2):221-34.
  • Mochida Y, Cabral H, Miura Y, Albertini F, Fukushima S, Osada K, Nishiyama N, Kataoka K. "Bundled assembly of helical nanostructures in polymeric micelles loaded with platinum drugs enhancing therapeutic efficiency against pancreatic tumor." ACS Nano. 2014 Jul 22;8(7):6724-38.
  • Krishnan N, Koveal D, Miller DH, Xue B, Akshinthala SD, Kragelj J, Jensen MR, Gauss C-M, Page R, Blackledge M, Muthuswamy SK, Peti W and Tonks N. "Targeting the disordered C terminus of PTP1B with an allosteric inhibitor." Nature Chem. Biol. 2014 10, 558–566
  • Hizukuri Y, Oda T, Tabata S, Tamura-Kawakami K, Oi R, Sato M, Takagi J, Akiyama Y, Nogi T. “A Structure-Based Model of Substrate Discrimination by a Noncanonical PDZ Tandem in the Intramembrane-Cleaving Protease RseP.” Structure 2014 22(2): 326-336

2013

  • Bonsor DA, Weiss E, Iosub-Amir A, Reingewertz TH, Chen TW, Haas R, Friedler A, Fischer W, Sundberg EJ. “Characterization of the translocation-competent complex between the Helicobacter pylori oncogenic protein CagA and the accessory protein CagF.” J Biol Chem. 2013 Nov 15;288(46):32897-909
  • Sana B, Johnson E, Le Magueres P, Criswell A, Cascio D, Lim S. “The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties.” J Biol Chem. 2013 Nov 8;288(45):32663-72
  • Sagane Y, Hayashi S, Matsumoto T, Miyashita S, Inui K, Miyata K, Yajima S, Suzuki T, Hasegawa K, Yamano A, Nishikawa A, Ohyama T, Watanabe T, Niwa K. “Sugar-induced conformational change found in the HA-33/HA-17 trimer of the botulinum toxin complex.” Biochem Biophys Res Commun. 2013 Aug 30;438(3):483-487
  • Ohbayashi N, Matsumoto T, Shima H, Goto M, Watanabe K, Yamano A, Katoh Y, Igarashi K, Yamagata Y, Murayama K. “Solution Structure of Clostridial Collagenase H and Its Calcium-Dependent Global Conformation Change.” Biophysical Journal (2013), 104(7) 1538–1545
  • Garces AP, Watowich SJ. “Intrinsic Flexibility of West Nile Virus Protease in Solution Characterized Using Small-Angle X-ray Scattering.” Biochemistry, 2013 52 (39), pp 6856-6865
  • He Q, Shumate CK, White MA, Molineux IJ, and Yin YW. “Exonuclease of human DNA polymerase gamma disengages its strand displacement function.” Mitochondrion 13 (2013) 592-601
  • Cherry AL, Finta C, Karlstro M, Jin Q, Schwend T, Astorga-Wells J, Zubarev RA, Del Campo M, Criswell AR, de Sanctis D, Jovine L, and Toftga R. “Structural basis of SUFU–GLI interaction in human Hedgehog signalling regulation.” Acta Cryst. (2013). D69, 2563-2579
  • Polizzi SJ, Walsh RM , Le Magueres P, Criswell AR, and Wood ZA. “Human UDP-α-d-xylose Synthase Forms a Catalytically Important Tetramer That Has Not Been Observed in Crystal Structures.” Biochemistry, 2013, 52(22): 3888-3898
  • Edwards JS, Betts L, Frazier ML, Pollet RM, Kwong SM, Walton WG, Bellentine WK III, Huang JJ, Habibi S, Del Campo M, Meier JL, Dervan PB, Firth N, Redinbo MR. “Molecular basis of antibiotic multiresistance transfer in Staphylococcus aureus.” PNAS. 2013 Feb 19;110(8):2804-9

2012

  • Sagane Y, Miyashita S, Miyata K, Matsumoto T, Inui K, Hayashi S, Suzuki T, Hasegawa K, Yajima S, Yamano A, Niwa K, Watanabe T. “Small-angle X-ray scattering reveals structural dynamics of the botulinum neurotoxin associating protein, nontoxic nonhemagglutinin.” Biochem Biophys Res Commun. 2012 Aug 24;425(2):256-260
  • Matsumoto T, Kinoshita T, Kirii Y, Tada T, Yamano A., “Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4.” Biochem Biophys Res Commun. 2012 Aug 24;425(2):195-200
  • Takekiyo T, Yamazaki K, Yamaguchi E, Abe H, Yoshimura Y. “High Ionic Liquid Concentration-Induced Structural Change of Protein in Aqueous Solution: A Case Study of Lysozyme.” J Phys Chem B, 2012, 116(36): 11092-11097
  • Zheng J, Gay DC, Demeler B, White MA, and Keitinge-Clay AT. “Divergence of multimodular polyketide synthases revealed by a didomain structure” Nat Chem Biol 2012 July; 8(7): 615-621

A video of the BioSAXS-2000, the protein small angle X-ray scattering system from Rigaku

If you are unable to view this video, click here to download it (338 MB).

OptiSAXS

Focuses and monochromatizes an X-ray beam for small angle X-ray scattering


Rigaku's OptiSAXS optic is the latest generation of Cofocal Max-Flux® (CMF) optic for the BioSAXS-2000nano SAXS system configured with a Rigaku microfocus rotating anode generator. The long length of the OptiSAXS optic allows it to capture more of the X-ray beam from the microfocus generator resulting in higher flux. As a result, the OptiSAXS optic delivers an intense, monochromatic X-ray beam with greater than two-fold higher flux compared to its predecessor.

Features

  • Graded, multilayer confocal optic with increased length for maximum beam intensity.
  • Double-bounce beam geometry for optimum beam purity
  • Designed to achieve maximum performance when coupled with Rigaku microfocus X-ray generators
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