The DLS instrument is not available from the 14/09/2020 until the 25/09/2020 included
Presentation
Dynamic Light Scattering (DLS) is used to measure particle size and molecule size. This technique measures the diffusion of particles moving under Brownian motion, and converts this to size and a size distribution using the Stokes-Einstein relationship.
Application
- Characterise the size/monodispersity of various particles including proteins and micelles
- Determination of molecular sizes (diameter 0.3nm to 10.0 microns)
- Detection of aggregates / oligomerisation
Key words
Dynamic Light Scattering, diffusion coefficient, monodispersity, polydispersity,
Staff
Manager: Caroline Mas
Office: CIBB room 020
Platform: CIBB room 001
Specific Equipment
Access mode
Users must read the conditions of use of the instruments as well as of the management of the services provided:
Location
The Biophysical platform is located in the Carl-Ivar Brändén Building, ground floor, room 001 (Shared Building C).
How to make a request
Short training on data collection will be done on the instrument with User’s samples ( 30 min)
- To make a BOOKING REQUEST, fill this REQUEST FORM HERE
- To make a TRAINING REQUEST: send an email to caroline.mas@ibs.fr
DLS Booking
Samples
Only non-pathogenic biological samples are accepted. Decree of the July 18, 1994 establishing the list of biological pathogens, amended by Decrees of April 17, 1997 and June 30, 1998 (Decrees in French). The list of biological pathogens is available on the website of the IPBS.
- Sample requirement :
- Purity of protein : <90%
- Volume : 45µl
- Don’t forget to bring your own cuvette!
Follow up / acknowledgements
The user agrees to promote the obtained results by mentioning the platform in the acknowledgements in case of publication or scientific communication and to communicate the reference of the article to the responsible for the platform.
Acknowledgements in publications:
Please find below the sentence that has to be written in all publications based on our UAR platforms:
« This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). We thank Caroline Mas for assistance and/or access to the biophysics platform. »
