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X-RAY EMISSION FROM MATERIALS PROCESSING LASERS.

ABSTRACT: The emission of laser induced X-rays from materials processing ultra-short pulsed laser systems was measured. The absolute spectral photon fluence was determined using a thermoluminescence detector based few-channel spectrometer. The spectra at 10 cm from the laser focus were in the energy region between 2 and 25 keV with mean energies of ~4-6 keV (when weighted by fluence or directional dose equivalent) and up to 13 keV (when weighted by ambient dose equivalent). The operational quantities, H·'(0.07), H·'(3) and H·*(10), were determined to be in the order of 1600-7300, 16-71 and 1-4 mSv per hour processing time, respectively, depending on the material and condition of the workpiece. The dose contribution due to photons above 30 keV was for all quantities negligible, i.e. below 10-3.

SUBMITTER: Behrens R

PROVIDER: S-EPMC6543886 | biostudies-other | 2019 May

REPOSITORIES: biostudies-other

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X-RAY EMISSION FROM MATERIALS PROCESSING LASERS.

Behrens R R Pullner B B Reginatto M M

Radiation protection dosimetry 20190501 3

The emission of laser induced X-rays from materials processing ultra-short pulsed laser systems was measured. The absolute spectral photon fluence was determined using a thermoluminescence detector based few-channel spectrometer. The spectra at 10 cm from the laser focus were in the energy region between 2 and 25 keV with mean energies of ~4-6 keV (when weighted by fluence or directional dose equivalent) and up to 13 keV (when weighted by ambient dose equivalent). The operational quantities, H·' ...[more]

PMID: 30215786

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Project description:Structural biology continues to benefit from an expanding toolkit, which is helping to gain unprecedented insight into the assembly and organization of multi-protein machineries, enzyme mechanisms and ligand/inhibitor binding. The combination of results from X-ray free-electron lasers (XFELs), modern synchrotron crystallographic beamlines and cryo-electron microscopy (cryoEM) is proving to be particularly powerful. The highly brilliant undulator beamlines at modern synchrotron facilities have empowered the crystallographic revolution of high-throughput structure determination at high resolution. The brilliance of the X-rays at these crystallographic beamlines has enabled this to be achieved using microcrystals, but at the expense of an increased absorbed X-ray dose and a consequent vulnerability to radiation-induced changes. The advent of serial femtosecond crystallography (SFX) with X-ray free-electron lasers provides a new opportunity in which damage-free structures can be obtained from much smaller crystals (2?µm) and more complex macromolecules, including membrane proteins and multi-protein complexes. For redox enzymes, SFX provides a unique opportunity by providing damage-free structures at both cryogenic and ambient temperatures. The promise of being able to visualize macromolecular structures and complexes at high resolution without the need for crystals using X-rays has remained a dream, but recent technological advancements in cryoEM have made this come true and hardly a month goes by when the structure of a new/novel macromolecular assembly is not revealed. The uniqueness of cryoEM in providing structural information for multi-protein complexes, particularly membrane proteins, has been demonstrated by examples such as respirasomes. The synergistic use of cryoEM and crystallography in lead-compound optimization is highlighted by the example of the visualization of antimalarial compounds in cytochrome bc 1. In this short review, using some recent examples including our own work, we share the excitement of these powerful structural biology methods.

Dataset Information

X-RAY EMISSION FROM MATERIALS PROCESSING LASERS.

Publications

X-RAY EMISSION FROM MATERIALS PROCESSING LASERS.

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