Structural Molecular Biology

Structural Molecular Biology

Illuminating Biological Structures at the Atomic and Molecular Levels

SMB

NIH
Click here to learn about capabilities available at other BER Structural Biology and Imaging Resources.

Structural Molecular Biology

The Structural Molecular Biology (SMB) Division and program enable scientists to rapidly obtain and utilize structural information on biomolecular and bioinspired systems at the atomic-to-micron scale, and at temporal resolutions, to understand function (and malfunction) in biological processes. Our goals range from innovative fundamental discovery-based science to applied uses, such as biotechnology, drug discovery, bioenergy and bioremediation. The SMB program has pioneered and will continue to lead development of new and enhanced techniques and facilities and make them widely and rapidly available to the biomedical, bioenergy, biogeochemical and environmental research communities.

The SMB program integrates macromolecular X-ray crystallography (MC), biological small/wide angle X-ray scattering/diffraction (SAXS/WAXS), µ-X-ray fluorescence (µXRF) imaging, and X-ray absorption (XAS) and emission spectroscopy (XES), across 8 beam lines, to holistically study the most challenging and wide-ranging biological systems.

We work closely with a broad community of scientists from academia, industry, and national laboratories in a commitment of collaboration, user support, training and education. At the core of the SMB program is a commitment to education of the future workforce through extensive outreach and training.

There is synergy with the LCLS X-ray free electron laser and the SLAC-Stanford cryo-electron microscopy (cryoEM) and cryo-electron tomography (cryoET) facilities and other advanced light and electron bioimaging programs across SLAC/SSRL. Collectively, this provides a remarkably rich and broad window on structure and function across a wide range of biologically relevant length and time scales, creating the foundation to extend results at the atomic and molecular level to understanding complex macromolecular interactions, and to studies of organelle, cell and tissue organization and function.

The SMB program engages with Stanford’s ChEM-H, with other user facilities and where relevant, lead multi-user-facility arrangements in areas that provide user access to complementary techniques, such as with the Environmental Molecular Science Laboratory (EMSL) and the Joint Genome Institute (JGI), and in a coordinated outreach program within BER-funded facilities and research groups.


SMB Programs

Macromolecular Crystallography

Macromolecular Crystallography is a technique used to study biological molecules such as proteins, viruses and nucleic acids to a spatial resolution at atomic level. This high resolution can provide the detailed mechanism by which these macromolecules carry out their functions in living cells and organisms.

Learn More

Biological Small Angle X-ray Scattering/Diffraction

Biological SAXS is a powerful probe for the structure and dynamics of proteins, nucleic acids, lipids and their complexes. It provides details at the molecular and nanoscale level in the physiologically relevant solution state of the biomolecules in action.

Learn More

 

X-ray Absorption and Emission Spectroscopy

The SMB BioXAS program provides a combination of powerful spectroscopy and imaging facilities to unravel atomic resolution local structure, electronic properties, distribution and speciation of metal ions and ligands in biology accelerating biomedical and bioenergy breakthroughs.

Learn More

Nobel

Nobel Prizes

The 2006 Noble Prize in Chemistry was awarded to Roger Kornberg for research carried out in part at SSRL. Kornberg revealed the process of transcription, through which DNA's genetic blueprint directs the manufacture of proteins.

Nobel Prizes

 

Due Dates

New Proposals & Extension Requests

Run PeriodX-Ray/VUVMacromolecular Crystallography
Quarter 1May 1April 1
Quarter 2August 1July 1
Quarter 3November 1December 1

Beam Time Requests

Run PeriodX-Ray/VUVMacromolecular Crystallography
Quarter 1August 1September 1
Quarter 2November 1January 20
Quarter 3February 22April 18

Partnerships & Collaborations

Image
Cryo-EM
Composite image of density map, 2.2 Å resolution map, and fitted atomic coordinates for the enzyme β-galactosidase, demonstrating the gradual increase in quality of the cryo-EM structures from low to high resolution.

Cryo-EM (Cryogenic Electron Microscopy) Facility

Cryo-EM generates 3-D images at nearly atomic resolution of viruses, molecules and complex biological machines inside the cell, such as the ribosomes where proteins are synthesized. By flash-freezing these tiny things in their natural environments, scientists can see how they are built and what they do in much more detail than before, stringing thousands of images together to create stop-action movies and even taking virtual “slices” through cells, much like miniature CT scans.

Cryo-EM Website

SLAC Biosciences Division

The Biosciences Division builds on SLAC’s unique strengths in X-ray based research to explore biological function on multiple scales, from individual genes, proteins and enzymes to molecular ecosystems. SLAC’s world-class capabilities in ultrafast and high-throughput macromolecular crystallography, small-angle x-ray scattering, imaging and spectroscopy are optimal for revealing the physical and electronic structures of macromolecules in particular – the cornerstones of biological systems.

SLAC Biosciences Website

Image
SLAC Biosciences Division
The combined protein complex at work in brain signaling is responsible for the calcium-triggered release of neurotransmitters from our brain’s nerve cells in a process called synaptic vesicle fusion. In the background, electrical signals travel through a neuron.
Image
MFX
Macromolecular Femtosecond Crystallography

Multi-User Facility Collaborations

SSRL and LCLS scientists have partnered to develop the Macromolecular Femtosecond Crystallography (MFX) instrument at LCLS, home to a dedicated and highly automated goniometer-based setup for serial femtosecond crystallography experiments, with similar experimental hardware and control software as SSRL microfocus beam lines 12-1/2. The LCLS X-ray free electron laser expands the structural information accessible from small radiation-sensitive crystals, including metalloenzyme intermediate states. Applying short (fs) X-ray pulses, diffraction is obtained before substantial radiation-induced atomic rearrangements occur within the crystals, enabling ultra-fast time-resolved measurements.

SMB Website

 


Contacts & Resources


Future Capabilities

SMB AreaDiffractionScatteringSpectroscopy & Imaging
Macromolecular CrystallographyMicro-Beam, Undulator for Micro- to Nano-CrystallographyMicro- to Nano-Crystallography Instrumentation at LCLS   
Biological SAXS  Microfocus Optics; High-Speed Detector  
Biological XAS and XES   New Detector ApproachesAdvanced Spectroscopy Undulator (XES, XRS, RIXS, HERFD/XAS)
Picosecond to Femtosecond Time Domain Micro- to Nano-Crystallography Instrumentation at LCLS  Advanced Spectroscopy Undulator (XES, XRS, RIXS) and LCLS