Publications by authors named "J M Beale"
The enterobacterial common antigen (ECA) is conserved in Gram-negative bacteria of the order although its function is debated. ECA biogenesis depends on the Wzx/Wzy-dependent strategy whereby the newly synthesized lipid-linked repeat units, lipid III, are transferred across the inner membrane by the lipid III flippase WzxE. WzxE is part of the Wzx family and required in many glycan assembly systems, but an understanding of its molecular mechanism is hindered due to a lack of structural evidence.
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- X-ray free-electron lasers (XFELs) are advancing time-resolved structural experiments, essential for understanding macromolecule functions and mechanisms.
- The SwissMX sample-delivery system was tested at SwissFEL using a micro-structured polymer chip, focusing on the light-sensitive protein LOV1 to avoid light contamination during pump-probe experiments.
- The opaque MISP chips enabled effective studies of LOV1's structural dynamics, confirming a crucial bond formation and suggesting potential for increased XFEL project efficiency by reducing protein sample usage.
Background: Total hip arthroplasty (THA) is increasingly used every year; however, there is currently limited information on factors that impact the length of stay (LOS) following the procedure. Longer LOS following THA is met with an increase in the cost of care, necessitating studies to identify factors that may impact LOS.
Methods: In this retrospective study, we used the Nationwide Inpatient Sample (NIS) database from 2016 to 2019 to analyze the preoperative comorbidities and postoperative complications that impact the LOS following THA.
Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs.
View Article and Find Full Text PDFPhotolyase is an enzyme that uses light to catalyze DNA repair. To capture the reaction intermediates involved in the enzyme's catalytic cycle, we conducted a time-resolved crystallography experiment. We found that photolyase traps the excited state of the active cofactor, flavin adenine dinucleotide (FAD), in a highly bent geometry.
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