Self starting additive pulse modelocking of a Nd:LMA laser

A Ti:sapphire-pumped Nd:LMA laser has been passively mode locked by using additive-pulse mode locking, which generates 600-fs-duration pulses at 1.054-µm. The wavelength, pulse duration, and long-term stability of the laser make it eminently suitable as a front-end oscillator of a high-power, chirped-pulse amplifier experiment based on 1.053-µm amplification in Nd:phosphate glass

Sub-picosecond pulse generation from a laser-diode pumped, self-starting additive-pulse mode-locked Nd:LMA laser

We report the generation of sub-picosecond mode-locked pulses at 1.05 µm from an additive-pulse mode-locked laser diode-pumped La1-xNdxMgAl11O19 laser. The repetition rate was 93 MHz, and the maximum average output power was 60 mW

Tracking Single Particles and Elongated Filaments with Nanometer Precision

Recent developments in image processing have greatly advanced our understanding of biomolecular processes in vitro and in vivo. In particular, using Gaussian models to fit the intensity profiles of nanometer-sized objects have enabled their two-dimensional localization with a precision in the one-nanometer range. Here, we present an algorithm to precisely localize curved filaments whose structures are characterized by subresolution diameters and micrometer lengths. Using surface-immobilized microtubules, fluorescently labeled with rhodamine, we demonstrate positional precisions of ∼2 nm when determining the filament centerline and ∼9 nm when localizing the filament tips. Combined with state-of-the-art single particle tracking we apply the algorithm 1), to motor-proteins stepping on immobilized microtubules, 2), to depolymerizing microtubules, and 3), to microtubules gliding over motor-coated surfaces

Side-binding proteins modulate actin filament dynamics

International audienceActin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of filaments to polymerize and depolymerize at their ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. In this study, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by the binding of proteins to the lateral filament surface. We also show that the pointed-end has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of flexibility as well as effects on fragmentation and growth suggest that the observed kinetic diversity arises from structural alteration. Tuning elongation kinetics by exploiting the malleability of the filament structure may be a ubiquitous mechanism to generate a rich variety of cellular actin dynamics