Pacific Northwest National Laboratory
The Environmental Molecular Sciences Laboratory (EMSL) is a DOE scientific user facility at the Pacific Northwest National Laboratory sponsored by the Biological and Environmental Research Program. EMSL advances and integrates process-level understanding of complex biological and environmental systems across wide temporal and spatial scales by coupling observations, experiments, and theory with modeling and simulation.
The biological research focus at EMSL is to understand, predict, manipulate, and design biological processes in microbial, fungal, and plant systems for bioenergy and bioproduct production and enhance the understanding of carbon, nutrient, and inorganic element transformations. The focus for fundamental environmental research is to characterize the structure and function of Earth systems to develop and validate predictive models by studying atmospheric chemistry and physics, vegetative ecosystems, and soil or subsurface hydrology and biogeochemistry.
Co-located BER Resources
EMSL hosts more than 150 experimental instruments that provide users with high-resolution spatiotemporal imaging and structural data to study biological and environmental systems at the molecular level. These instruments, in combination with EMSL’s supercomputing capabilities, have helped thousands of researchers use a multidisciplinary, collaborative approach to solve important challenges in biological interactions and dynamics, biogeochemistry and subsurface science, and interactions at the interfaces of natural and engineered materials.
Structural biology expertise at EMSL includes a breadth of cutting-edge capabilities. Combining these with high-performance computing and complementary expertise in other areas enables correlative multimodal imaging and analysis.
- High-resolution cryo-electron microscopy determines the atomic-scale structure of proteins and protein complexes to uncover the molecular mechanisms regulating cellular processes.
- Cryo-electron tomography characterizes cellular ultrastructure in microbial systems, providing clues to how organisms respond within a microbial consortium or to environmental stresses.
- Nuclear magnetic resonance spectroscopy measures the distance between protons to determine the structure of small proteins less than 30 kDa.
- Mass spectrometry examines the organizational relationship between protein complex subunits and their post-translational modifications, providing insights into the molecular mechanisms driving enzymatic reactions in these complexes.
- Cryogenic atom probe tomography produces three-dimensional maps of elements and molecular fragments at the atomic scale and is being adapted to soft biological materials.