A beamstop device recently developed at the ALS has successfully combined two essential crystallographic functions–capturing the damaging portion of the beam while simultaneously monitoring its intensity–into a single miniaturized package. The technology has been licensed and launched commercially and is also a finalist for an R&D 100 Award. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
Validation of Novel Proteins Inspired by Nature
Designed proteins containing hydrogen-bonding modules have been validated by crystallography and SAXS. The ability to design synthetic molecules that combine the specificity of DNA-like binding with protein function opens up huge opportunities for the fields of synthetic biology and materials science. Read more »
How Antidepressants Block Serotonin Transport
Malfunctions in the complex protein “machinery” of serotonin transport can result in depression, obsessive-compulsive disorder, aggression, anxiety, and Parkinson’s disease. Now, researchers have obtained x-ray crystallographic structures of the difficult-to-crystallize human serotonin transporter bound to two commonly prescribed antidepressant drug molecules. Read more »
Understanding the Key to Henipavirus Infection
The Hendra virus was the first member of the genus Henipavirus, an emergent group of viruses with a high mortality rate. Knowledge of the protein structure that mediates Hendra entry into host cells could enable the design of antigens with improved immunogenic response. Read more »
Reducing Plant Lignin for Cheaper Biofuels
Scientists have identified and validated a novel approach to reducing lignin in plants by tweaking a key lignin enzyme. Their technique could help lower the cost of converting biomass into carbon-neutral fuels to power cars and other sustainably developed bio-products. Read more »
Shutting Out Ebola and Other Viruses
Researchers have used protein crystallography at the ALS to understand how a drug molecule that has shown some efficacy against Ebola in mice inactivates a membrane protein, called TPC1, used by viruses to infect host cells. Read more »
Exploring the Repeat-Protein Universe
Researchers have published a landmark study that used both crystallography and SAXS to validate computationally designed structures of novel proteins with repeated motifs. The results show that the protein-folding universe is far larger than realized, opening up a wide array of new possibilities for biomolecular engineering. Read more »
Improving Anti-Influenza Medications
Protein crystallography at ALS Beamline 8.3.1 helped scientists understand the M2 proton-channel structure from the influenza A virus, an understanding that is needed to design better anti-influenza medications. Read more »
Improving Meningococcal Vaccines
Scientists have found a way to improve the stability of an essential antigenic protein to develop vaccines with higher efficacy for prevention of bacterial meningitis. Read more »
Foreign DNA Capture during CRISPR–Cas Adaptive Immunity
Using macromolecular crystallography at Beamline 8.3.1 at the ALS, Berkeley researchers discovered how CRISPR/Cas captures foreign DNA for the bacterial immune system. Read more »