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Rigaku Corporation Small Angle X-Ray Scattering (SAXS) Kratky Camera System BioSAXS-1000

Description
Macromolecular crystallography and NMR are two of the most important techniques for furthering our understanding of structural biology. However, the fact remains that three-dimensional structures derived from NMR and single crystal analysis are difficult to achieve at best and quite often the analyses fail. The time, energy and money spent on cloning, expressing and purifying proteins that refuse to crystallize or are inappropriate for NMR analysis, drive up the overall cost of structural biology research and if a project is abandoned when a structure cannot be produced, the efforts are totally wasted. Small angle X-ray scattering (SAXS) is a technique that can be applied to solutions of macromolecules to determine a variety of molecular properties, most of which are related to the shape of the molecule. The information acquired is useful both pre- and post-structure determination, making it a synergetic technique for structural biologists. You can determine the molecular weight of the molecule/complex in solution, which in turn tells you the oligomeric state in solution. You can tell if the sample is mono-disperse or aggregated. You can tell if a protein is folded, unfolded or contains disordered regions. You can determine a low resolution, three-dimensional shape of the molecule/complex, which can be used for a variety of modeling purposes. Rigaku's new BioSAXS-1000 SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-1000 takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-1000 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. Compared to a standard Kratky camera that utilizes the line focus from a standard sealed tube source, the BioSAXS-1000 is equipped with a doubly focusing multilayer optic assembly that produces a more brilliant beam at the sample. Since the beam is focused on the detector, there is no need to de-smear the data. Moreover, data from the BioSAXS-1000 rivals SAXS data collected at the synchrotron with data collection times usually 30 minutes or less.

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Small Angle X-Ray Scattering (SAXS) Kratky Camera System - BioSAXS-1000 - Rigaku Corporation
The Woodlands, TX, USA
Small Angle X-Ray Scattering (SAXS) Kratky Camera System
BioSAXS-1000
Small Angle X-Ray Scattering (SAXS) Kratky Camera System BioSAXS-1000
Macromolecular crystallography and NMR are two of the most important techniques for furthering our understanding of structural biology. However, the fact remains that three-dimensional structures derived from NMR and single crystal analysis are difficult to achieve at best and quite often the analyses fail. The time, energy and money spent on cloning, expressing and purifying proteins that refuse to crystallize or are inappropriate for NMR analysis, drive up the overall cost of structural biology research and if a project is abandoned when a structure cannot be produced, the efforts are totally wasted. Small angle X-ray scattering (SAXS) is a technique that can be applied to solutions of macromolecules to determine a variety of molecular properties, most of which are related to the shape of the molecule. The information acquired is useful both pre- and post-structure determination, making it a synergetic technique for structural biologists. You can determine the molecular weight of the molecule/complex in solution, which in turn tells you the oligomeric state in solution. You can tell if the sample is mono-disperse or aggregated. You can tell if a protein is folded, unfolded or contains disordered regions. You can determine a low resolution, three-dimensional shape of the molecule/complex, which can be used for a variety of modeling purposes. Rigaku's new BioSAXS-1000 SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-1000 takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-1000 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. Compared to a standard Kratky camera that utilizes the line focus from a standard sealed tube source, the BioSAXS-1000 is equipped with a doubly focusing multilayer optic assembly that produces a more brilliant beam at the sample. Since the beam is focused on the detector, there is no need to de-smear the data. Moreover, data from the BioSAXS-1000 rivals SAXS data collected at the synchrotron with data collection times usually 30 minutes or less.

Macromolecular crystallography and NMR are two of the most important techniques for furthering our understanding of structural biology. However, the fact remains that three-dimensional structures derived from NMR and single crystal analysis are difficult to achieve at best and quite often the analyses fail. The time, energy and money spent on cloning, expressing and purifying proteins that refuse to crystallize or are inappropriate for NMR analysis, drive up the overall cost of structural biology research and if a project is abandoned when a structure cannot be produced, the efforts are totally wasted.

Small angle X-ray scattering (SAXS) is a technique that can be applied to solutions of macromolecules to determine a variety of molecular properties, most of which are related to the shape of the molecule. The information acquired is useful both pre- and post-structure determination, making it a synergetic technique for structural biologists. You can determine the molecular weight of the molecule/complex in solution, which in turn tells you the oligomeric state in solution. You can tell if the sample is mono-disperse or aggregated. You can tell if a protein is folded, unfolded or contains disordered regions. You can determine a low resolution, three-dimensional shape of the molecule/complex, which can be used for a variety of modeling purposes.

Rigaku's new BioSAXS-1000 SAXS camera is designed specifically to meet the needs of the structural biologist. Based on a patented two-dimensional Kratky design, the BioSAXS-1000 takes up much less space than a conventional 3-pinhole camera but offers better flux characteristics. Best of all, the BioSAXS-1000 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.

Compared to a standard Kratky camera that utilizes the line focus from a standard sealed tube source, the BioSAXS-1000 is equipped with a doubly focusing multilayer optic assembly that produces a more brilliant beam at the sample. Since the beam is focused on the detector, there is no need to de-smear the data. Moreover, data from the BioSAXS-1000 rivals SAXS data collected at the synchrotron with data collection times usually 30 minutes or less.

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Technical Specifications

  Rigaku Corporation
Product Category Diffractometers
Product Number BioSAXS-1000
Product Name Small Angle X-Ray Scattering (SAXS) Kratky Camera System
Features Benchtop
Wave X-Ray
Detector Camera
Diffraction Method Powder; Single Crystal
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