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User Resources for NSLS-II operations and experiments during COVID-19

National Synchrotron Light Source II

NSLS-II is a state-of-the-art 3 GeV electron storage ring. The facility offers scientific and industrial researchers an array of beamlines with x-ray, ultraviolet, and infrared light to enable discoveries in clean and affordable energy, high-temperature superconductivity, molecular electronics, and more. Overview »

 

The next deadline for NSLS-II beam time proposals and beam time requests is May 31, 2021.  |   Submission Details

Become a Facility User

Beamlines at the National Synchrotron Light Source II are open to academic and industrial users for scientific research. All research proposals are subjected to peer review and ranked against competing proposals based on scientific merit.

NSLS-II Beamlines

NSLS-II’s beamlines and experimental stations offer unique, cutting-edge research tools for a wide variety of scientific areas. All beamlines are organized into five science programs, based on the research capabilities and expertise they offer.


Full Calendar

Seminars

  1. APR

    21

    Wednesday

    Center for Biomolecular Structure Lecture Series

    "Lanthanide-Binding Tags for 3D X-Ray Imaging of Proteins in Cells at Nanoscale Resolution"

    Presented by Lisa Miller, Brookhaven National Laboratory - NSLS II

    1:30 pm, Videoconference / Virtual Event

    Wednesday, April 21, 2021, 1:30 pm

    Hosted by: Vivian Stojanoff

    In order to get the link to join the event you will need to register. X-ray Fluorescence Microscopy (XFM) is a powerful method for imaging the trace-element concentration, distribution, and speciation in cells and tissues. Even though the technique has been around for more than 30 years, only recently have advances in X-ray sources, optics, and detectors enabled two- and three-dimensional X-ray imaging at the nanoscale with attogram detection sensitivity. However, one limitation of XFM for imaging biological systems is detecting the trace-element distribution in the context of subcellular organelles and individual proteins. For visible light microscopy, the most ubiquitous method for imaging individual proteins within the context of a living cell is the use of intrinsically fluorescent proteins, such as the green fluorescent protein (GFP) that is co-expressed as a fusion tag along with the protein of interest. However, visualization of these tags is limited by the wavelengths of visible light except by applying specialized super resolution approaches. Here, we are developing applications enabled by encoded lanthanide-binding tags (LBTs), which are GFP-like analogs of minimal size (ca. 15-20 amino acids) for XFM. In this talk, applications of LBTs to both membrane-bound and cytosolic proteins will be demonstrated in 2D and 3D using a 15 nm X-ray beam. This approach enables visualization of LBT-tagged proteins while simultaneously measuring the elemental distribution in cells at a spatial resolution necessary for visualizing cell membranes and eukaryotic subcellular organelles.

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Conferences & Workshops

  1. MAY

    17

    Monday

    NSLS-II & CFN Joint Users' Meeting

    May 17-20, 2021

  2. AUG

    25

    Wednesday

    Workshop on Resonant Inelastic and Elastic X-ray Scattering 2021

    August 25-27, 2021

  3. NOV

    17

    Wednesday

    Short Course: Introduction to X-ray Absorption Fine Structure 2021

    November 17-19, 2021

 

Science ProgramsDetails

Complex Scattering

Hard X-ray Scattering & Spectroscopy

Imaging and Microscopy

Soft X-ray Scattering & Spectroscopy

Structural Biology

User Services Office

Brookhaven National Laboratory
743 Brookhaven Avenue
Building 743
Upton, NY 11973-5000

(631) 344-8737 | nsls2user@bnl.gov | website

Visiting NSLS-II

If you are a contractor or vendor coming to NSLS-II for the day, please work with your host to gain access to the Lab site. If you will be on site for more than one day, please contact the Guest, User, and Visitor Center for access and training requirements. See maps and directions for getting here.