Room temperature serial oscillation crystallography
Serial crystallography is a method for obtaining structural information on an atomic level of a protein, without the need for large protein crystals. Instead, small diffraction datasets are collected on many small protein crystals, which are usually easier to obtain than large ones. Serial crystallography is an ideal method for collecting diffraction data of proteins at room temperature, where the onset of radiation damage from the X-ray beam is rapid.
Study offers new target for antibiotic resistant bacteria
As antibiotic resistance rises, the search for new antibiotic strategies has become imperative. In 2013, the Centers for Disease Control estimated that antibiotic resistant bacteria cause at least 2 million infections and 23,000 deaths a year in the U.S.; a recent report raised the likely mortality rate to 162,044.
CHESS Users Meeting Workshop on "Biomolecules Under Pressure"
There is growing interest in the biological research community to characterize and understand the impact of high pressures, i.e. 100s of MPa, on the physical properties and function of biological macromolecules, e.g. proteins, viruses, lipids etc.
First Crystal Structure at CHESS beamline ID7B2
In one of the first commissioning experiments since the upgrade of the facility, the team of Aaron Finke and collaborators measured the first crystal structure at CHESS beamline ID7B2. The beamline provided excellent quality data and a good refined structure from a fluoroacetate dehalogenase crystal was obtained as shown below. Further commissioning is underway. Even at this early stage, ID7B2 is definitely geared up to be a world-class beamline.
First Light at CHESS
First Light at CHESS into Sector 7B2 Hutch!
Predicting X-ray solution scattering from flexible macromolecules
Proteins are molecular machines that participate in the vast majority of activities that occur in any living system. To carry out their functions, they undergo dynamic changes in structure and shape and interact with other molecular systems. Characterizing these intramolecular motions provides insight into the molecular basis of protein function and, in turn, can result in a deeper understanding of a vast range of physiological functions.
Solving protein structure from sparse serial microcrystal diffraction data at a storage ring synchrotron source
X-ray crystallography allows determination of the atomic structure of proteins, information that is essential to understanding the proteins. It was thought that there was a minimum size of crystal that could be used at storage ring x-ray sources. This paper shows that the minimum size barrier can be overcome.
A naturally occurring antibiotic active against drug-resistant tuberculosis
A naturally occurring antibiotic called kanglemycin A is effective against Mycobacterium tuberculosis, the bacteria that cause tuberculosis, even in drug-resistant strains, according to an international team of researchers who used chemistry, molecular biology, microbiology, and X-ray crystallography to show how the compound maintains its activity.