Corrigendum to “High-speed atomic force microscopy: Imaging and force spectroscopy” [FEBS Lett. 588 (19) (2014) 3631-3638]

FEBS Letters ◽  
2015 ◽  
Vol 589 (12) ◽  
pp. 1389-1389
Author(s):  
F. Eghiaian ◽  
F. Rico ◽  
A. Colom ◽  
I. Casuso ◽  
S. Scheuring
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Force Spectroscopy ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging

High-speed atomic force microscopy: Imaging and force spectroscopy

FEBS Letters ◽  
2014 ◽  
Vol 588 (19) ◽  
pp. 3631-3638 ◽  
Author(s):  
Frédéric Eghiaian ◽  
Felix Rico ◽  
Adai Colom ◽  
Ignacio Casuso ◽  
Simon Scheuring
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Force Spectroscopy ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging

scholarly journals High-speed dynamic-mode atomic force microscopy imaging of polymers: an adaptive multiloop-mode approach

2017 ◽  
Vol 8 ◽  
pp. 1563-1570 ◽  
Author(s):  
Juan Ren ◽  
Qingze Zou
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Interaction Force ◽  
Dynamic Mode ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Mode Tm ◽  
Mode Atomic Force Microscopy

Adaptive multiloop-mode (AMLM) imaging to substantially increase (over an order of magnitude) the speed of tapping-mode (TM) imaging is tested and evaluated through imaging three largely different heterogeneous polymer samples in experiments. It has been demonstrated that AMLM imaging, through the combination of a suite of advanced control techniques, is promising to achieve high-speed dynamic-mode atomic force microscopy imaging. The performance, usability, and robustness of the AMLM in various imaging applications, however, is yet to be assessed. In this work, three benchmark polymer samples, including a PS–LDPE sample, an SBS sample, and a Celgard sample, differing in feature size and stiffness of two orders of magnitude, are imaged using the AMLM technique at high-speeds of 25 Hz and 20 Hz, respectively. The comparison of the images obtained to those obtained by using TM imaging at scan rates of 1 Hz and 2 Hz showed that the quality of the 25 Hz and 20 Hz AMLM imaging is at the same level of that of the 1 Hz TM imaging, while the tip–sample interaction force is substantially smaller than that of the 2 Hz TM imaging.

scholarly journals High-speed atomic force microscopy imaging of live mammalian cells

2017 ◽  
Vol 14 (0) ◽  
pp. 127-135 ◽  
Author(s):  
Mikihiro Shibata ◽  
Hiroki Watanabe ◽  
Takayuki Uchihashi ◽  
Toshio Ando ◽  
Ryohei Yasuda
Keyword(s):  
Atomic Force Microscopy ◽  
Mammalian Cells ◽  
High Speed ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging

Feed-Forward Compensation for High-Speed Atomic Force Microscopy Imaging of Biomolecules

2006 ◽  
Vol 45 (3B) ◽  
pp. 1904-1908 ◽  
Author(s):  
Takayuki Uchihashi ◽  
Noriyuki Kodera ◽  
Hisanori Itoh ◽  
Hayato Yamashita ◽  
Toshio Ando
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Microscopy Imaging ◽  
Feed Forward ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging

scholarly journals Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin

2015 ◽  
Vol 290 (34) ◽  
pp. 20793-20803 ◽  
Author(s):  
Wilaiwan Sriwimol ◽  
Aratee Aroonkesorn ◽  
Somsri Sakdee ◽  
Chalermpol Kanchanawarin ◽  
Takayuki Uchihashi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Bacillus Thuringiensis ◽  
High Speed ◽  
Three Dimensional ◽  
Molecular Assembly ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Trimer Formation

The insecticidal feature of the three-domain Cry δ-endotoxins from Bacillus thuringiensis is generally attributed to their capability to form oligomeric pores, causing lysis of target larval midgut cells. However, the molecular description of their oligomerization process has not been clearly defined. Here a stable prepore of the 65-kDa trypsin-activated Cry4Ba mosquito-specific toxin was established through membrane-mimetic environments by forming an ∼200-kDa octyl-β-d-glucoside micelle-induced trimer. The SDS-resistant trimer caused cytolysis to Sf9 insect cells expressing Aedes-mALP (a Cry4Ba receptor) and was more effective than a toxin monomer in membrane perturbation of calcein-loaded liposomes. A three-dimensional model of toxin trimer obtained by negative-stain EM in combination with single-particle reconstruction at ∼5 nm resolution showed a propeller-shaped structure with 3-fold symmetry. Fitting the three-dimensional reconstructed EM map with a 100-ns molecular dynamics-simulated Cry4Ba structure interacting with an octyl-β-d-glucoside micelle showed relative positioning of individual domains in the context of the trimeric complex with a major protrusion from the pore-forming domain. Moreover, high-speed atomic force microscopy imaging at nanometer resolution and a subsecond frame rate demonstrated conformational transitions from a propeller-like to a globularly shaped trimer upon lipid membrane interactions, implying prepore-to-pore conversion. Real-time trimeric arrangement of monomers associated with l-α-dimyristoylphosphatidylcholine/3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulfonic acid bicelle membranes was also envisaged by successive high-speed atomic force microscopy imaging, depicting interactions among three individual subunits toward trimer formation. Together, our data provide the first pivotal insights into the structural requirement of membrane-induced conformational changes of Cry4Ba toxin monomers for the molecular assembly of a prepore trimer capable of inserting into target membranes to generate a lytic pore.

scholarly journals High-frequency multimodal atomic force microscopy

2014 ◽  
Vol 5 ◽  
pp. 2459-2467 ◽  
Author(s):  
Adrian P Nievergelt ◽  
Jonathan D Adams ◽  
Pascal D Odermatt ◽  
Georg E Fantner
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
High Frequency ◽  
High Speed ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nanoscale Topography ◽  
Atomic Force Microscopy Imaging ◽  
Speed Method

Multifrequency atomic force microscopy imaging has been recently demonstrated as a powerful technique for quickly obtaining information about the mechanical properties of a sample. Combining this development with recent gains in imaging speed through small cantilevers holds the promise of a convenient, high-speed method for obtaining nanoscale topography as well as mechanical properties. Nevertheless, instrument bandwidth limitations on cantilever excitation and readout have restricted the ability of multifrequency techniques to fully benefit from small cantilevers. We present an approach for cantilever excitation and deflection readout with a bandwidth of 20 MHz, enabling multifrequency techniques extended beyond 2 MHz for obtaining materials contrast in liquid and air, as well as soft imaging of delicate biological samples.

scholarly journals Dynamic remodeling of the dynamin helix during membrane constriction

2017 ◽  
Vol 114 (21) ◽  
pp. 5449-5454 ◽  
Author(s):  
Adai Colom ◽  
Lorena Redondo-Morata ◽  
Nicolas Chiaruttini ◽  
Aurélien Roux ◽  
Simon Scheuring
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Lateral Displacement ◽  
Microscopy Imaging ◽  
Gtp Hydrolysis ◽  
Force Microscopy ◽  
Membrane Fission ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Lateral Displacements

Dynamin is a dimeric GTPase that assembles into a helix around the neck of endocytic buds. Upon GTP hydrolysis, dynamin breaks these necks, a reaction called membrane fission. Fission requires dynamin to first constrict the membrane. It is unclear, however, how dynamin helix constriction works. Here we undertake a direct high-speed atomic force microscopy imaging analysis to visualize the constriction of single dynamin-coated membrane tubules. We show GTP-induced dynamic rearrangements of the dynamin helix turns: the average distances between turns reduce with GTP hydrolysis. These distances vary, however, over time because helical turns were observed to transiently pair and dissociate. At fission sites, these cycles of association and dissociation were correlated with relative lateral displacement of the turns and constriction. Our findings show relative longitudinal and lateral displacements of helical turns related to constriction. Our work highlights the potential of high-speed atomic force microscopy for the observation of mechanochemical proteins onto membranes during action at almost molecular resolution.

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