An MFP-3D-Bio Atomic Force Microscope (AFM, Asylum Research) was used to obtain images with an SNL probe (Bruker) under tapping mode at room temperature (22 °C). Mfp-3s and COL1A1 was deposited on a mica surface (area ~ 1 cm2) by adsorbing 50 μL of the protein from a 20 μg/ml mfp3s concentration or a 25 μg/ml of COL1A1 concentration in buffer solution at pH 3.0 or 7.5.
Snl probe
Manufactured by Bruker
Sourced in United States
The SNL probes are a range of scanning near-field optical microscopy (SNOM) probes developed by Bruker. They are designed to enable high-resolution optical imaging and spectroscopy on a variety of sample types. The core function of the SNL probes is to provide a means for optical signal collection and delivery at the nanoscale.
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Lab products found in correlation
Mfp 3d bio atomic force microscope, by Oxford Instruments (1 mentions)
Agilent 5500 microscope, by Agilent Technologies (1 mentions)
Multimode afm, by Veeco (1 mentions)
Picoview software, by Agilent Technologies (1 mentions)
Agilent 5500, by Agilent Technologies (1 mentions)
Multimode 8 atomic force microscope, by Bruker (1 mentions)
6 protocols using snl probe
1
Atomic Force Microscopy of Mfp-3S and COL1A1
2
AFM Visualization of Oregon Green® 488 DHPE and DMPC Adsorption on Mica
3
Elasticity Profiling of OMVs by AFM
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AFM measurements were performed with an Agilent 5500 microscope (Agilent, Santa Clara, CA, USA), working in contact and tapping mode, under the control of PicoView software as previously described53 (link). OMVs were immobilized on freshly cleaved mica, with poly-L-lysine as a stabilizing matrix. We used SNL probes (Bruker Corp., Billerica, MA, USA) with nominal k = 0.35 N/m. For elasticity determination, the k constant of each probe was measured with a built-in Agilent Thermal-K setup.
Surface probing for elasticity determination was done with a built-in plugin for PicoView software, recording and analyzing force-distance curves. Usually, a resolution of 32 × 32 was used for probing over a chosen region of about 1.5 μm × 1.5 μm. The average elasticity of pixels correlating to grains was measured in the overall image, and then the values from several images for each sample were averaged (n > 25). For AFM analysis the same amount of pure OMVs was used.
Images were analyzed with Gwydion 2.61 software54 (link),55 (link). The size of OMVs was measured by manual selection using the “line” Gwydion tool, which measures the distance between two points—at least one hundred counts were measured for each type of OMVs.
Surface probing for elasticity determination was done with a built-in plugin for PicoView software, recording and analyzing force-distance curves. Usually, a resolution of 32 × 32 was used for probing over a chosen region of about 1.5 μm × 1.5 μm. The average elasticity of pixels correlating to grains was measured in the overall image, and then the values from several images for each sample were averaged (n > 25). For AFM analysis the same amount of pure OMVs was used.
Images were analyzed with Gwydion 2.61 software54 (link),55 (link). The size of OMVs was measured by manual selection using the “line” Gwydion tool, which measures the distance between two points—at least one hundred counts were measured for each type of OMVs.
4
Fluid Tapping Mode AFM Imaging
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AFM images were taken in fluid tapping mode with a Multimode AFM (Veeco Metrology Group) using a Nanoscope V controller. Silicon nitride cantilevers with 2 nm radius silicon tips were used (SNL probes from Bruker).
5
Atomic Force Microscopy of Plastoglobules
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AFM measurements were performed with an Agilent 5500 (Agilent Technologies Inc., Santa Clara, CA, USA) microscope, working in contact and tapping modes, under the control of PicoView software (Agilent Technologies Inc., Santa Clara, CA, USA). Samples were imaged in a liquid cell, and SNL probes (Bruker Corp., Billerica, MA, USA) with nominal k = 0.35 N/m were used. For elasticity determination, the k constant of each probe was measured with a built-in Agilent Thermal-K setup. Plastoglobule samples were immobilised on freshly cleaved mica, with poly-L-lysine used as stabilising matrix.
Images were recorded at 1 ln/s and resolution 512 × 512, with minimal possible force applied. Surface probing for elasticity determination was done with a built-in plugin for PicoView software, recording and analysing force-distance curves. Usually, a resolution of 32 × 32 was used for probing a chosen region of approximately 2 μm × 2 μm. Images were processed with Gwyddion 2.49 software [79 (link),80 (link)].
Images were recorded at 1 ln/s and resolution 512 × 512, with minimal possible force applied. Surface probing for elasticity determination was done with a built-in plugin for PicoView software, recording and analysing force-distance curves. Usually, a resolution of 32 × 32 was used for probing a chosen region of approximately 2 μm × 2 μm. Images were processed with Gwyddion 2.49 software [79 (link),80 (link)].
6
Nanoscale Imaging of Biomolecular Complexes
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A MultiMode 8 atomic force microscope (Bruker) was used for imaging SAMs and the topology of patterned proteins. Lateral force microscopy (LFM) imaging of photopatterned SAMs was conducted in air at ambient conditions using triangular SNL probes (Bruker) with a nominal spring constant of approximately 0.12 Nm−1 and a nominal resonant frequency of around 23 kHz. Immobilized nanopatterned RC-LH1-PufX and LHCII complexes were imaged in PeakForceTapping mode at nearly physiological conditions in buffer (PBS, pH 7.4), at room temperature using SNL probes (Bruker) with a nominal spring constant of approximately 0.35 Nm−1 and a nominal resonant frequency of around 18 kHz (in liquid). The modulation amplitude and frequency were adjusted to values in the range 20–24 nm and 2 kHz, respectively.
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