# Structural Dynamics at LCLS

> **NIH NIH P41** · STANFORD UNIVERSITY · 2021 · $674,285

## Abstract

ABSTRACT: TR&D-1
To enable beamtime at the oversubscribed LCLS source to be used for scientific discovery, not
experiment optimization, the activities under this TR&D are aimed at developing the tools
necessary to fully prepare for biomedical experiments and to characterize samples both before
and during LCLS beam time. This ranges from understanding the sample quality and properties,
as well as the state of the sample during complex sample delivery, or during a dynamic process
being studied. The existing capabilities of SLAC will be enhanced via this TR&D, providing new
tools in sample preparation and characterization, as well as new diagnostics to understand the
state of the sample. Furthermore, capabilities at SSRL will be leveraged and augmented to use
the synchrotron X-ray beam as a key tool to prepare for LCLS beamtime and for new science.
Finally, spectroscopic capabilities for sample characterization at LCLS will be expanded.
The proposed TR&D scope is at the cutting-edge of the biomedical structural biology field by
exploiting X-ray FEL capabilities to solve new structures and study the dynamics of molecules
under near-physiological conditions at ambient temperatures. The proposed developments will
make use of state-of-the-art X-ray FEL capabilities and complement them with offline capabilities
that themselves represent cutting-edge advances. The TR&D will increase the combined
technologies’ impact on biomedical research by providing higher readiness levels to LCLS
experiments for higher quality data in a shorter time. By increasing efficiency, the “extra” beam
time access will be used for additional higher-risk, higher-reward experiments. It will also allow
more rapid access to solve emerging scientific questions. By taking X-ray FEL sample preparation
and delivery from an art to a quantitative science, it is expected that LCLS and this BTRR will
have a significant impact in the structure determination of complexes and membrane proteins,
provide accurate active site structures of metalloenzymes, and provide enhanced and more
broadly available capabilities to observe macromolecular dynamics using the combined powers
of LCLS and SSRL.

## Key facts

- **NIH application ID:** 10089009
- **Project number:** 1P41GM139687-01
- **Recipient organization:** STANFORD UNIVERSITY
- **Principal Investigator:** Mark Hunter
- **Activity code:** P41 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2021
- **Award amount:** $674,285
- **Award type:** 1
- **Project period:** 2021-04-01 → 2026-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10089009

## Citation

> US National Institutes of Health, RePORTER application 10089009, Structural Dynamics at LCLS (1P41GM139687-01). Retrieved via AI Analytics 2026-05-22 from https://api.ai-analytics.org/grant/nih/10089009. Licensed CC0.

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