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Related Concept Videos

Atomic Force Microscopy01:08

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...
Studying the Cytoskeleton01:17

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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...

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Related Experiment Video

Updated: Jun 22, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy.

Henriette Jensenius1, Dionne C G Klein, Martin van Hecke

  • 1Leiden Institute of Physics, Leiden University, Niels Bohrweg 2, Leiden, The Netherlands.

Journal of Molecular Biology
|June 9, 2009
PubMed
Summary
This summary is machine-generated.

Mannan-binding lectin (MBL) exhibits a unique "sertiform" structure, differing from the typical "bouquet" model. This finding clarifies the MBL pathway

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Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

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Related Experiment Videos

Last Updated: Jun 22, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy
09:48

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Published on: February 27, 2015

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Mannan-binding lectin (MBL) is a key pathogen recognition molecule in innate immunity.
  • MBL initiates complement activation upon binding to microbial surfaces.
  • Previous models depicted MBL with a "bouquet-like" quaternary structure.

Purpose of the Study:

  • To elucidate the tertiary and quaternary structures of Mannan-binding lectin (MBL).
  • To compare the observed MBL structure with existing models and related complement proteins.

Main Methods:

  • Atomic force microscopy (AFM) was employed to visualize MBL structure.
  • Structural analysis was performed in both air and buffer conditions.
  • Image analysis focused on subunit association angles and kinked arm conformations.

Main Results:

  • MBL displays a "sertiform" quaternary structure, characterized by a central hub with fanning subunits.
  • Subunit association angle is predominantly 40 degrees, stable in oligomers of four or more subunits.
  • Approximately 30% of MBL subunits exhibit a kinked arm conformation around 145 degrees.

Conclusions:

  • The observed "sertiform" structure of MBL contrasts with the previously assumed "bouquet-like" model.
  • Structural insights provide a basis for understanding MBL's role in complement activation.
  • The flexibility and conformation of MBL are crucial for its immune function.