After decades of effort, scientists have revealed atomic-scale details of the water splitting step of photosynthesis, the chemical process that generates the air we breathe. The latest work adds to our understanding of photosynthesis and will aid the development of fully renewable alternative energy sources.
Nicholas Sauter, a computer senior scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, is co-leading a team working to provide a better way for scientists to study the structures of the many materials that don’t form tidy single crystals. Their new technique, called small-molecule serial femtosecond X-ray crystallography, or smSFX, supercharges traditional crystallography with the addition of custom-built image processing algorithms and an X-ray free electron laser (XFEL). In a paper published in Nature, the team demonstrated proof-of-principle for smSFX and reported the previously unknown structures of two metal-organic materials known as chacogenolates.
As part of an international collaboration, researchers at Lawrence Berkeley National Laboratory (Berkeley Lab), the Diamond Light Source synchrotron facility, and Oxford and Bristol Universities in England have developed a novel sample delivery system that expands the limited toolkit for performing dynamic structural biology studies of enzyme catalysis, which have so far mostly been limited to a small number of light-driven enzymes.
X-ray free-electron lasers (XFELs) came into use in 2010 for protein crystallography, allowing scientists to study fully hydrated specimens at room temperature without radiation damage. Researchers have developed many new experimental and computational techniques to optimize the technology and draw the most accurate picture of proteins from crystals. Now scientists in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division have developed a new program, diffBragg, which can process every pixel collected from an XFEL for a protein structure independently. In a recent IUCrJ paper, the team led by MBIB Senior Scientist Nicholas Sauter proposed a new processing framework for more accurate determination of protein structures.
An international team led by researchers in Berkeley Lab’s Molecular Biophysics and Integrated Bioimaging (MBIB) Division has revealed a key step in the molecular mechanism behind the water splitting reaction of photosynthesis. The finding could help inform the design of renewable energy technology.