BioSAXS-2000ⁿᵃⁿᵒ

BioSAXS-2000ⁿᵃⁿᵒ
Kratky SAXS for proteins and macromolecules Kratky SAXS for proteins and macromolecules Kratky SAXS for proteins and macromolecules
Features
  • Easily installed on the open port of an existing generator or can be installed with your choice of X-ray source: Microfocus sealed tube, MicroMax-007 HF, FR-X
  • Point focusing optics eliminates smearing issues common to traditional Kratky cameras.
  • All system components are motorized for control from control computer
  • Photodiode beamstop for intensity measurements and sample absorption correction
  • Sample temperature control included with system
  • 2D Kratky collimation allows one to achieve low q measurements with no realignment
  • SAXSLab data collection and processing software

Small angle X-ray scattering (SAXS) Kratky camera system

Small angle scattering of macromolecules

Learn More  

Rigaku's BioSAXS-2000nano SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-2000nano takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-2000nano can be mounted on the open port of a Rigaku rotating anode X-ray generator, taking full advantage of existing infrastructure, or it can be mated to a Rigaku microfocus sealed tube X-ray source. The BioSAXS AUTO configuration incorporates two time-saving features: an Automatic Sample Changer for unattended overnight operation and an Automatic Analysis Pipeline based on the world standard ATSAS package from EMBL Hamburg.

No need to wait for beamtime at a synchrotron

The BioSAXS-2000nano is equipped with the new OptiSAXS optic, a doubly focusing multilayer optic whose focus is at the detector. The OptiSAXS provides better than two fold improvement in flux compared to its predecessor resulting in higher brilliance at the sample position and data collection times in the range of minutes. Thus, the BioSAXS-2000nano brings a beamline experience to home laboratory SAXS experiments.

Optional accessories

  • Automatic Sample Changer (ASC) with support for up to 96 samples.
  • Automatic Analysis Pipeline (AAP) based on ATSAS, the world’s most popular SAXS analysis software developed at EMBL Hamburg.

Specifications

Product name BioSAXS-2000nano
Technique Biological small angle scattering
Benefit Home-lab SAXS camera
Technology 2-dimensional Kratky SAXS
Core attributes Compact design, OptiSAXS optics, 2-D Kratky collimation
Core options

Automatic Sample Changer
Automatic Analysis Pipeline (AAP) based on ATSAS
Computer External PC, MS Windows® OS, 
Core dimensions Varies with configuration
Mass Varies with configuration
Power requirements Varies with configuration

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
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