Sample-Scanning High-Speed
Atomic Force Microscope "SS-NEX" - Ando model -




NanoExplorer (NEX)


Dynamic Visualization of nano-scale world

HS-AFM*1.0 - Ando model - is the High-Speed Atomic Force Microscope which was developed based on the research achievements accomplished by Prof. Ando in Kanazawa University. This is the world’s first instrument that broke through the weak point of conventional AFM “low-speed”, and realized the video rate scan. The high-speed scan enables us to capture swinging molecules in solution clearly without blurring. Consequently, the strong anchoring of a sample to the substrate is unnecessary and a dynamic observation is achieved without losing the activities of soft biomolecules.


*The HS-AFM was developed by Prof. Ando (Kanazawa Univ.) and commercialized by RIBM.


Walking_myosinV
Walking_myosinV
bacteriorhodopsin (D96N)
rotorless F1-ATPase
walking myosin V(realtime)
bacteriorhodopsin
in response to light(x10)
rotorless F1-ATPase(realtime)

Contents


High-speed scanner

  • Active dumping and counter balance can suppress mechanical vibration.
  • Compact and reliable design

In addition to Standard high-speed scanner, specialized scanners:

Injection type, Ultra high-speed, Wide scanner are optionally available.

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Ultra small and soft cantilever with high resonance frequency

  • Cantilever for HS-AFM can realize the observation of any soft samples such as a protein.
 

Ultra small cantilever

Resonance frequency :1500 kHz (in air )

Force constant :0.1 N/m

Tip radius :< 10 nm

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High-speed and stable feedback control

  • Clear and fine images of surface structures can be obtained by using the high-speed scanning.

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Standard system Specifications

Scan Speed 50 ms / frame (20 frames / sec)
Piezo Range X: 0.7 μm, Y: 0.7 μm, Z: 0.4 μm
Sample Size 1.5 mm in diameter
Detection Method Optical lever method
Scanning Method Sample scan
Environment In liquid / In air
Control System PID control, Dynamic PID control
Measurement Mode AC mode. Topography and phase image
Significant Function Scanner active dumping
Drift correction for cantilever excitation

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Options

  • Units
Light irradiation Unit Light irradiation unit for the experiments with caged compounds.
Variable wavelength : 350 - 560 nm
Circulation unit The observation solutions can be exchanged while continuing AFM observation. The pH value and/or the buffer composition can be gradually changed during the measurement.
Heat control unit From room temperature to 50℃
*Under developments

  • Scanners
Standard scanner Suitable for observing reactions between molecules .
  • Scan Speed : 50 ms / frame (20 frames / sec)
  • Scan Range : XY : 0.7 μm × 0.7 μm, Z : 0.4 μm
Wide scanner Suitable for relatively large samples with a high scanning rate.
  • Scan Speed : 1 s / frame (1 frame / sec)
  • Scan Range : XY : 4 μm × 4 μm, Z : 0.7 μm
Mechanically amplified
ultra wider scanner
Suitable for observing whole body of large samples such as cells.
  • Scan Speed : 10 s / frame (0.1 frames / sec)
  • Scan Range : XY : 30 μm × 30 μm, Z : 1.2 μm
  • Each scan range is typical value.
  • Maximum scanning rate is for a specific measurement condition.

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Movie Gallery

IgG

IgG antibodies


Dynamic Imaging of the IgG antibodies
DNA

Plasmid DNA


Dynamic Imaging of the Plasmid DNA on the mica-substrate
DNase

Dynamic Imaging of the DNA digestion process by DNase


(DNA : λDNA , DNase: endonuclease)
DNA digestion by Nuclease

DNA digestion by Nuclease


Dynamic Imaging of the DNA digestion process
(DNA : pUC18 plasmid DNA , DNA digestion: Bal31 nuclease)
DNA Polymerase reaction

DNA Polymerase reaction


Dynamic Imaging of the DNA elongation process with Phi29 in liquid
(DNA:λDNA , DNA polymerase: Phi29)
Point defect in streptavidin 2D crystal

Point defect in streptavidin 2D crystal


Dynamic Imaging of the diffusion on point defects in the crystal

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Image Gallery

IgG
plasmid DNA
myosinⅡ
IgG antibody
150nm * 150nm
Standard high-speed scanner
plasmid DNA
250nm * 250nm
Standard high-speed scanner
myosinⅡ
500nm * 500nm
Standard high-speed scanner
streptavidin
GroEL
bacteriorhodopsin
streptavidin
90nm * 90nm
(*1)
GroEL
90nm * 90nm
(*1)
bacteriorhodopsin
40nm * 40nm
(*1)
lipid membrane
350nm Beads
350nm Beads
lipid membrane
3500nm * 3500nm
Wide scanner
350nm polystyrene beads
3000nm * 3000nm
Wide scanner
350nm polystyrene beads
900nm * 900nm
Wide scanner
ecoli
E.coli
3000nm * 3000nm
Wide scanner

(*1) Image courtesy of Prof. Ando (Kanazawa Univ.)


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Published Papers

Video imaging of walking myosin V




a. and b. : Direct observation of walking myosin V. a. 130 nm x 65 nm, b. 125 nm x 62.5 nm. c. Scheme of myosin V walking.


Myosin V is a two-headed processive motor and functions as cargo transporter in cells. The dynamic behaviors of myosin V translocating along actin filaments were visualized by HS-AFM. The high-resolution movies provided not only ‘visual evidence’ for previously speculated or demonstrated molecular behaviors, including lever-arm swing, but also more detailed behaviors of the molecules, leading to a comprehensive understanding of the motor mechanism. This direct and dynamic high-resolution visualization is a powerful new approach to studying the structure and dynamics of biomolecules in action.

N. Kodera et al. Nature 468, 72 (2010). Kanazawa University


Dynamic molecular processes in photoactivated bacteriorhodopsin



Structural change of bacteriorhodopsin (bR), which is known as light-driven proton pump, has been visualized by HS-AFM. The purple membrane composed of D96N bR mutant, which has a longer photocycle (10’s) than that of the wild type, was adsorbed on mica substrate. Upon illumination with green light (532nm), bR drastically changes its structure and returns to the unphotolysed state in a few seconds after light-off. This outcome is reproducible in repeated dark illumination cycles.

M. Shibata et al. Nature Nanotech. 5, 208 (2010). Kanazawa University


Point defect in streptavidin 2D crystal




a. Dynamic observation of the diffusion of point defects. b. Scheme of streptavidin arrays in a C222 crystal. Unit lattice vectors are indicated by red arrows.


The diffusion of point defects in the crystals was successfully observed by HS-AFM. In Figure a, the trajectory tracking of two monovacancy defects was obviously anisotropic with respect to the two axes of the crystalline lattice. As a result, the diffusion constant D along each axis could be established to be Da = 20.5 nm2/s and Db = 48.8 nm2/s. This means, HS-AFM is useful for studying various dynamic process, such as the crystal growth and disintegration processes.

D. Yamamoto et al. Nanotechnology 19, 384009 (2008). Kanazawa University

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Reference List

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Contact

Research Institute of Biomolecule Metrology Co.,Ltd.
1-17-1 Sengen, Tsukuba, Ibaraki 305-0047, Japan
TEL: +81-29-896-6500, FAX: +81-29-896-6501
E-mail: world-sales@ribm.co.jp

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