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1.
Phys Rev Lett ; 119(25): 255002, 2017 Dec 22.
Article in English | MEDLINE | ID: mdl-29303310

ABSTRACT

We investigate the formation of a laser-produced magnetized jet under conditions of a varying mass ejection rate and a varying divergence of the ejected plasma flow. This is done by irradiating a solid target placed in a 20 T magnetic field with, first, a collinear precursor laser pulse (10^{12} W/cm^{2}) and, then, a main pulse (10^{13} W/cm^{2}) arriving 9-19 ns later. Varying the time delay between the two pulses is found to control the divergence of the expanding plasma, which is shown to increase the strength of and heating in the conical shock that is responsible for jet collimation. These results show that plasma collimation due to shocks against a strong magnetic field can lead to stable, astrophysically relevant jets that are sustained over time scales 100 times the laser pulse duration (i.e., >70 ns), even in the case of strong variability at the source.

2.
Nat Commun ; 12(1): 762, 2021 Feb 03.
Article in English | MEDLINE | ID: mdl-33536408

ABSTRACT

The shaping of astrophysical outflows into bright, dense, and collimated jets due to magnetic pressure is here investigated using laboratory experiments. Here we look at the impact on jet collimation of a misalignment between the outflow, as it stems from the source, and the magnetic field. For small misalignments, a magnetic nozzle forms and redirects the outflow in a collimated jet. For growing misalignments, this nozzle becomes increasingly asymmetric, disrupting jet formation. Our results thus suggest outflow/magnetic field misalignment to be a plausible key process regulating jet collimation in a variety of objects from our Sun's outflows to extragalatic jets. Furthermore, they provide a possible interpretation for the observed structuring of astrophysical jets. Jet modulation could be interpreted as the signature of changes over time in the outflow/ambient field angle, and the change in the direction of the jet could be the signature of changes in the direction of the ambient field.

3.
Phys Rev E ; 101(4-1): 043208, 2020 Apr.
Article in English | MEDLINE | ID: mdl-32422777

ABSTRACT

The formation of high energy density matter occurs in inertial confinement fusion, astrophysical, and geophysical systems. In this context, it is important to couple as much energy as possible into a target while maintaining high density. A recent experimental campaign, using buried layer (or "sandwich" type) targets and the ultrahigh laser contrast Vulcan petawatt laser facility, resulted in 500 Mbar pressures in solid density plasmas (which corresponds to about 4.6×10^{7}J/cm^{3} energy density). The densities and temperatures of the generated plasma were measured based on the analysis of x-ray spectral line profiles and relative intensities.

4.
J Cell Biol ; 143(2): 351-8, 1998 Oct 19.
Article in English | MEDLINE | ID: mdl-9786947

ABSTRACT

Mitochondria exist as a dynamic tubular network with projections that move, break, and reseal in response to local environmental changes. We present evidence that a human dynamin-related protein (Drp1) is specifically required to establish this morphology. Drp1 is a GTPase with a domain structure similar to that of other dynamin family members. To identify the function of Drp1, we transiently transfected cells with mutant Drp1. A mutation in the GTPase domain caused profound alterations in mitochondrial morphology. The tubular projections normally present in wild-type cells were retracted into large perinuclear aggregates in cells expressing mutant Drp1. The morphology of other organelles was unaffected by mutant Drp1. There was also no effect of mutant Drp1 on the transport functions of the secretory and endocytic pathways. By EM, the mitochondrial aggregates found in cells that were transfected with mutant Drp1 appear as clusters of tubules rather than a large mass of coalescing membrane. We propose that Drp1 is important for distributing mitochondrial tubules throughout the cell. The function of this new dynamin-related protein in organelle morphology represents a novel role for a member of the dynamin family of proteins.


Subject(s)
Fungal Proteins/metabolism , GTP Phosphohydrolases/metabolism , GTP Phosphohydrolases/physiology , Microtubules/physiology , Mitochondria/enzymology , Saccharomyces cerevisiae Proteins , Animals , Biological Transport/physiology , COS Cells/chemistry , COS Cells/ultrastructure , Cloning, Molecular , Cytoplasmic Granules/chemistry , Cytoplasmic Granules/metabolism , Dynamin I , Dynamins , Endocytosis/physiology , Fungal Proteins/genetics , GTP Phosphohydrolases/genetics , Gene Expression Regulation, Enzymologic , Humans , Microscopy, Electron , Mitochondria/ultrastructure , Mitochondrial Proteins , Mutagenesis/physiology , Transfection
5.
J Mol Biol ; 171(4): 561-9, 1983 Dec 25.
Article in English | MEDLINE | ID: mdl-6363711

ABSTRACT

Freeze-dried and shadowed Escherichia coli 50 S ribosomal subunits have been examined by electron microscopy and a model of the subunit has been constructed. High resolution shadow casting has enabled us to determine independently the absolute hand of the subunit and to reveal some new structural features.


Subject(s)
Escherichia coli/ultrastructure , Ribosomes/ultrastructure , Freeze Drying , Microscopy, Electron , Models, Structural
6.
FEBS Lett ; 311(1): 22-4, 1992 Oct 12.
Article in English | MEDLINE | ID: mdl-1356830

ABSTRACT

A stable complex of the chaperonins, cpn60 and cpn10 (Escherichia coli GroEL and GroES homologues), from the extremely thermophilic bacterium Thermus thermophilus has been isolated and crystallized. The crystals have dimensions up to 30 x 200 x 200 microns. Ultra-thin sections of the crystals estimated by electron microscopy showed a rectangular lattice with unit cell parameters of a = 17 nm, b = 27 nm, gamma = 90 degrees.


Subject(s)
Bacterial Proteins/isolation & purification , Heat-Shock Proteins/isolation & purification , Proteins/isolation & purification , Thermus thermophilus/chemistry , Bacterial Proteins/ultrastructure , Chaperonin 10 , Chaperonin 60 , Chaperonins , Crystallization , Heat-Shock Proteins/ultrastructure , Macromolecular Substances , Proteins/ultrastructure
7.
FEBS Lett ; 275(1-2): 221-5, 1990 Nov 26.
Article in English | MEDLINE | ID: mdl-2261992

ABSTRACT

Human immunoglobulin G1 Van was studied by negative staining, freeze drying and high resolution shadow casting. The Fab and Fc subunits of an intact IgG1 molecule were shown to possess limited mobility. It was found that about 70% of molecules in the IgG1 Van specimen are not flat but have a tripod-like shape.


Subject(s)
Immunoglobulin G/ultrastructure , Humans , Immunoglobulin Fab Fragments/ultrastructure , Microscopy, Electron , Myeloma Proteins , Protein Conformation
8.
FEBS Lett ; 244(2): 291-5, 1989 Feb 27.
Article in English | MEDLINE | ID: mdl-2920829

ABSTRACT

Non-precipitating anti-dinitrophenyl pig immunoglobulins G have been studied by negative staining, freeze-drying and high-resolution shadow casting. The general morphology of the molecules is described. The predominant conformation of antibody molecules is a tripod-like one.


Subject(s)
Dinitrophenols/immunology , Immunoglobulin G , Animals , Freeze Drying , Immunoglobulin G/isolation & purification , Microscopy, Electron , Protein Conformation , Swine
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