A new experimental station in development at SLAC will expand capabilities for atomic-scale explorations in human health, biology, energy and environmental science.
Researchers have discovered that some common messenger molecules in human cells double as hormones when joined to a protein that interacts with DNA.
SSRL protein crystallography expert joined research effort that could lead to a safe and effective alternative to chemotherapy.
Scientists have for the first time mapped the atomic structure of a protein within a living cell. The technique, which peered into cells with an X-ray laser, could allow scientists to explore some components of living cells as never before.
Even in their infancy, X-ray lasers such as SLAC's Linac Coherent Light Source are notching a list of important discoveries, and a special issue of a scientific journal highlights their unique contributions to biological sciences.
By finding surprising similarities in the way immune system defenders bind to disease-causing invaders, a new study may help scientists develop new treatments.
Given a year to mature, the Institute for Chemical Biology is relaunching under a new name that better reflects its vision of bringing Stanford's unique interdisciplinary culture to bear at a new frontier of chemistry.
Five years ago, the brightest source of X-rays on the planet lit up at SLAC. The Linac Coherent Light Source (LCLS) X-ray laser's scientific and technical progress since its momentous "first light" have been no less luminous, say those who have played a role in its success.
A new tool for analyzing mountains of data from SLAC’s Linac Coherent Lightsource (LCLS) X-ray laser can produce high-quality images of important proteins using fewer samples. Scientists hope to use it to reveal the structures and functions of proteins that have proven elusive, as well as mine data from past experiments for new information
Researchers have used one of the brightest X-ray sources on the planet to map the 3-D structure of an important cellular gatekeeper known as a G protein-coupled receptor, or GPCR, in a more natural state than possible before.