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

Protein solution structure determination

BioSAXS-2000

Rigaku's BioSAXS-2000 SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-2000 takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-2000 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-2000 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-2000 brings a beamline experience to home laboratory SAXS experiments.

Optional accessories

  • Automatic Sample Changer (ASC) with support for 8 or 96 samples. See Accessories tab for more details.
  • Automatic Analysis Pipeline (AAP) based on ATSAS, the world’s most popular SAXS analysis software developed at EMBL Hamburg. See Accessories tab for more details.

Features

  • Automated sample stage with 3 capillary cells and one powder standard position
  • Simultaneous SAXS and WAXS measurements in a single image (qmax = 0.65 Å⁻¹)
  • 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

  • Camera Length: 500 mm
  • Sample Volume: 15 – 25 μL
  • Beam size at Sample: Variable Width x 1.5 mm²
  • Incident Beam: OptiSAXS CMF focusing optic
  • Collimation: 2D Kratky block (motorized)
  • Sample Stage: X, Y sample stage (motorized) with capacity for 3 sample capillaries, 1 standard powder position
  • Beam Stop: Horizontal movement (motorized) with PIN diode detector
  • q-range: 0.006 Å⁻¹ - 0.65 Å⁻¹
  • Detector: Dectris Pilatus 100K with reversed biased silicon diode array (active area: 83.8 mm X 33.5 mm)
  • Sample Temperature Control

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.

Automatic Sample Handling

The ASC provides unattended sample mounting and data collection for those labs who want to take advantage of the higher throughput capabilities offered by the BioSAXS-2000. The ASC supports samples supplied in 96-well plates or 0.2 mL PCR tube arrays and seamlessly integrates with the hardware and SAXSLab software control package. Solution samples can be foil-sealed to ensure that your samples won’t evaporate prior to data collection. The ASC also includes support for temperature controlled sample storage and for multiple cleaning solutions and cleaning protocols.

Automatic Data Analysis Pipeline

The AAP utilizes the industry standard ATSAS package to provide the following automatic analyses for each sample:
  • Automatic sample evaluation and aggregation identification
  • Automatic profile averaging and buffer subtraction
  • Automatic Guinier plot generation and calculation of Rg and I(0)
  • Automatic Kratky plot generation
  • Automatic Porod volume and molecular weight (MW) calculation
  • Automatic P(r) calculation with report of real space Rg and Dmax
  • Automatic envelope calculation, averaging and analysis
  • PDF report generator and easy review of previous AAP runs
The AAP thus allows for quick evaluation of sample quality, with color-coded results so that you can easily identify well-behaving samples versus those that exhibit aggregation and concentration effects.


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.

2014

  • 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

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

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

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-2000 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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