Kleinwinkelröntgenstreuung (SAXS) Kratky Kamerasystem

2018

• 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

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

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