For AFM imaging of Rec114–Mei4 or Mer2 bound to plasmid DNA, protein complexes were diluted to the indicated concentration (12–50 nM) in the presence of 1 nM supercoiled pUC19 in 25 mM HEPES-NaOH pH 6.8, 5 mM MgCl2, 50 mM NaCl, 10% glycerol. Complexes were assembled at 30 °C for 30 minutes. A volume of 40 μl of the protein-DNA binding reaction was deposited onto freshly cleaved mica (SP1) for 2 minutes. The sample was rinsed with 10 ml ultrapure deionized water and the surface was dried using a stream of nitrogen. AFM images were captured using an Asylum Research MFP-3D-BIO (Oxford Instruments) microscope in tapping mode at room temperature. An Olympus AC240TS-R3 AFM probe with resonance frequencies of approximately 70 kHz and spring constant of approximately 1.7 N/m was used for imaging. Images were collected at a speed of 0.5–1 Hz with an image size of 2 μm at 2048 × 2048 pixel resolution.
Asylum research mfp 3d bio
Manufactured by Oxford Instruments
The Asylum Research MFP-3D-BIO is a high-performance atomic force microscope (AFM) designed for biological applications. It provides a stable and precise platform for imaging and characterizing a wide range of biological samples in their native environments.
Automatically generated - may contain errors
Lab products found in correlation
3 protocols using asylum research mfp 3d bio
1
AFM Imaging of Protein-DNA Complexes
2
Visualizing R-loop-Containing Plasmids by AFM
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
A 50 μL reaction containing 10 nM linearized R-loop-containing plasmid/22 nM RPA/5% glycerol/0.3 mM ATP/10 mM Mg(OAc)2/100 mM KOAc/25 mM Hepes-KOH pH 7.5 was incubated on ice for 3 min; 40 μL of this reaction were deposited onto freshly cleaved mica for 2 min. The sample was rinsed with 10 mL ultrapure deionized water and the surface was dried using a stream of nitrogen. AFM images were captured using an Asylum Research MFP-3D-BIO (Oxford Instruments) microscope in tapping mode at room temperature. An Olympus AC240TS-R3 AFM probe with resonance frequencies of approximately 70 kHz and spring constant of approximately 1.7 N/m was used for imaging. Images were collected at a speed of 0.5–1 Hz with an image size of 2–3 μm at a 2048 × 2048 pixel resolution.
3
AFM Imaging of Protein-DNA Complexes
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
For AFM imaging of Rec114–Mei4 or Mer2 bound to plasmid DNA, protein complexes were diluted to the indicated concentration (12–50 nM) in the presence of 1 nM supercoiled pUC19 in 25 mM HEPES-NaOH pH 6.8, 5 mM MgCl2, 50 mM NaCl, 10% glycerol. Complexes were assembled at 30 °C for 30 minutes. A volume of 40 μl of the protein-DNA binding reaction was deposited onto freshly cleaved mica (SP1) for 2 minutes. The sample was rinsed with 10 ml ultrapure deionized water and the surface was dried using a stream of nitrogen. AFM images were captured using an Asylum Research MFP-3D-BIO (Oxford Instruments) microscope in tapping mode at room temperature. An Olympus AC240TS-R3 AFM probe with resonance frequencies of approximately 70 kHz and spring constant of approximately 1.7 N/m was used for imaging. Images were collected at a speed of 0.5–1 Hz with an image size of 2 μm at 2048 × 2048 pixel resolution.
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!