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The highly automated macromolecular crystallography beamline AMX/17-ID-1 is an undulator-based high-intensity (>5 × 10 photons s), micro-focus (7 µm × 5 µm), low-divergence (1 mrad × 0.35 mrad) energy-tunable (5-18 keV) beamline at the NSLS-II, Brookhaven National Laboratory, Upton, NY, USA. It is one of the three life science beamlines constructed by the NIH under the ABBIX project and it shares sector 17-ID with the FMX beamline, the frontier micro-focus macromolecular crystallography beamline. AMX saw first light in March 2016 and started general user operation in February 2017. At AMX, emphasis has been placed on high throughput, high capacity, and automation to enable data collection from the most challenging projects using an intense micro-focus beam. Here, the current state and capabilities of the beamline are reported, and the different macromolecular crystallography experiments that are routinely performed at AMX/17-ID-1 as well as some plans for the near future are presented.
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http://dx.doi.org/10.1107/S1600577522009377 | DOI Listing |
Biomolecules
July 2025
Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, F-38044 Grenoble, France.
AAA+ ATPases are ring-shaped hexameric protein complexes that operate as elaborate macromolecular motors, driving a variety of ATP-dependent cellular processes. AAA+ ATPases undergo large-scale conformational changes that lead to the conversion of chemical energy from ATP into mechanical work to perform a wide range of functions, such as unfolding and translocation of the protein substrate inside a proteolysis chamber of an AAA+-associated protease. Despite extensive biochemical studies on these macromolecular assemblies, the mechanism of substrate unfolding and degradation has long remained elusive.
View Article and Find Full Text PDFCommun Biol
August 2025
Molecular Imaging Center, The Fifth Affiliated Hospital, Sun Yat-sen University, Zhuhai, Guangdong, China.
The transition of SARS-CoV-2 into a recurrent, seasonal pathogen has underscored the need for the induction of durable immune protection. The nucleocapsid (N) protein is regarded as a promising complementary target for therapeutic and vaccine strategies, owing to its structural robustness, clinical relevance, and ability to elicit critical immune response. Within the N protein, the C-terminal domain (N-CTD) plays a pivotal role in assembly of viral RNA (vRNA)-N protein complexes, and in facilitating liquid-liquid phase separation (LLPS) through specific interactions with RNA on its dimerization surface.
View Article and Find Full Text PDFChem Sci
August 2025
Department of Chemistry, Indian Institute of Technology Delhi New Delhi 110016 India
Despite being a ubiquitous functional group with biological significance, thiols remain underexplored for their ability to form intermolecular interactions - especially in the solid state. This knowledge gap is largely due to the inadequacy of conventional X-ray crystallography in accurately locating protons involved in such weak thiol hydrogen bonds. Here, we explore weak thiol hydrogen bonds, using X-ray quantum crystallography (QCr) in a series of 31 thiol crystal structures.
View Article and Find Full Text PDFMolecules
August 2025
Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Sienkiewicza 112, 90-363 Lodz, Poland.
In this study, a series of novel alkoxylated resorcinarenes were synthesized using secondary and tertiary alcohols under mild catalytic conditions involving iminodiacetic acid. Structural characterization, including single-crystal X-ray diffraction, confirmed the successful incorporation of branched alkyl chains and highlighted the influence of substitution patterns on molecular packing. Notably, detailed mass spectrometric analysis revealed that, under specific conditions, the reaction pathway may shift toward the formation of defined oligomeric species with supramolecular characteristics-an observation that adds a new dimension to the synthetic potential of this system.
View Article and Find Full Text PDFbioRxiv
July 2025
Biosciences and Biotechnology Division, Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, USA.
The advent of ultrabright fourth generation X-ray light sources, including X-ray free-electron lasers (XFELs) and diffraction limited synchrotrons, has significantly advanced the field of serial macromolecular protein crystallography (SX). SX experiments demand a continuous supply of fresh microcrystalline sample, ideally while minimizing overall sample consumption. Here, we introduce a novel, robust, and user-friendly polymer film technology that can be assembled in various configurations to encapsulate protein microcrystals and provide sample support for SX.
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