A suite-level review of the neutron single-crystal diffraction instruments at Oak Ridge National Laboratory

Coates, Leighton; Cao, Huibo; Chakoumakos, Bryan C.; Frontzek, Matthias; Hoffmann, Christina; Kovalevsky, Andrey; Liu, Yaohua; Meilleur, Flora; Santos, A. M. dos; Myles, Dean A. A.; Wang, Xiaoping; Ye, Feng

doi:10.1063/1.5030896

Cited by 56 publications

(38 citation statements)

References 30 publications

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“…3.1. Neutron and X-ray room-temperature data collection Crystals were initially screened for diffraction quality using a broad-bandpass Laue configuration using neutrons from 2.8 to 10 Å wavelength at the IMAGINE instrument (Coates et al, 2018;Schrö der et al, 2018) at the High Flux Isotope Reactor (HFIR) at Oak Ridge National Laboratory (Fig. 4a).…”

Section: Resultsmentioning

confidence: 99%

“…The observed strong neutron diffraction indicated that the crystal was single and worthy of complete data collection. Neutron diffraction data were then collected using the time-of-flight (TOF; Langan et al, 2008) technique on the Macromolecular Neutron Diffractometer (MaNDi) instrument (Coates et al, 2010(Coates et al, , 2015(Coates et al, , 2018 at the Spallation Neutron Source (SNS) because the geometry of the MaNDi diffractometer provides better reciprocal-space coverage for the low-symmetry monoclinic space group. The crystal was held stationary at room temperature, and diffraction data (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Kneller

Phillips

Kovalevsky

et al. 2020

Acta Crystallogr F Struct Biol Commun

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The replication of SARS-CoV-2 produces two large polyproteins, pp1a and pp1ab, that are inactive until cleavage by the viral chymotrypsin-like cysteine protease enzyme (3CL Mpro) into a series of smaller functional proteins. At the heart of 3CL Mpro is an unusual catalytic dyad formed by the side chains of His41 and Cys145 and a coordinated water molecule. The catalytic mechanism by which the enzyme operates is still unknown, as crucial information on the protonation states within the active site is unclear. To experimentally determine the protonation states of the catalytic site and of the other residues in the substrate-binding cavity, and to visualize the hydrogen-bonding networks throughout the enzyme, room-temperature neutron and X-ray data were collected from a large H/D-exchanged crystal of ligand-free (apo) 3CL Mpro.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Kneller

Phillips

Kovalevsky

et al. 2020

Acta Crystallogr F Struct Biol Commun

View full text Add to dashboard Cite

show abstract

“…[44][45][46] Neutron diffraction data were collected using the Macromolecular Neutron Diffractometer (MaNDi) instrument at the Spallation Neutron Source (SNS). 45,[47][48][49] The crystal was held still at room temperature, and diffraction data were collected for 24 hours using all neutrons between 2-4 Å.…”

Section: Methodsmentioning

confidence: 99%

Protonation states in SARS-CoV-2 main protease mapped by neutron crystallography

Kneller

Phillips

Weiss

et al. 2020

Preprint

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The main protease (3CL Mpro) from SARS-CoV-2, the etiological agent of COVID-19, is an essential enzyme for viral replication, possessing an unusual catalytic dyad composed of His41 and Cys145. A long-standing question in the field has been what the protonation states of the ionizable residues in the substrate-binding active site cavity are. Here, we present the room-temperature neutron structure of 3CL Mpro from SARS-CoV-2, which allows direct determination of hydrogen atom positions and, hence, protonation states. The catalytic site natively adopts a zwitterionic reactive state where His41 is doubly protonated and positively charged, and Cys145 is in the negatively charged thiolate state. The neutron structure also identified the protonation states of other amino acid residues, mapping electrical charges and intricate hydrogen bonding networks in the SARS-CoV-2 3CL Mpro active site cavity and dimer interface. This structure highlights the ability of neutron protein crystallography for experimentally determining protonation states at near-physiological temperature — the critical information for structure-assisted and computational drug design.

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“…Single Crystal Neutron Diffraction : Time‐of‐flight single‐crystal neutron diffraction was performed on the TOPAZ diffractometer at the Spallation Neutron Source (Oak Ridge National Laboratory) . The crystal was mounted on a MiTeGen loop using a small amount of Super Glue.…”

Section: Methodsmentioning

confidence: 99%

Narrow Emission from Rb₃Sb₂I₉ Nanoparticles

Johnston

Dinic

Todorovič

et al. 2019

Advanced Optical Materials

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Metal halide perovskites have gained attention for their optoelectronic properties and are employed as the active layer in solar cells, light‐emitting diodes, and photodetectors. However, the use of lead in the best‐performing perovskite devices may limit their wider application. Prior reports of lead‐free perovskite nanoparticles have exhibited linewidths more than twice as wide as their lead‐halide counterparts, limiting their attainable color gamut. Here the solution synthesis of lead‐free Rb3Sb2I9 nanoplatelets and single crystals is reported; the single crystals exhibit broad (full‐width at half‐maximum (FWHM) = 75 nm) photoluminescence centered at 635 nm, while the nanoplatelets exhibit narrow emission (FWHM = 21 nm) at 512 nm. The photoluminescence quantum yield of both the single crystals and nanoplatelets is low and the present demonstration of the narrowest emission among all lead‐free perovskites reported to date motivates further study of how these and related materials can achieve further‐enhanced brightness.

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A suite-level review of the neutron single-crystal diffraction instruments at Oak Ridge National Laboratory

Cited by 56 publications

References 30 publications

Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Protonation states in SARS-CoV-2 main protease mapped by neutron crystallography

Narrow Emission from Rb₃Sb₂I₉ Nanoparticles

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A suite-level review of the neutron single-crystal diffraction instruments at Oak Ridge National Laboratory

Cited by 56 publications

References 30 publications

Room-temperature neutron and X-ray data collection of 3CL Mprofrom SARS-CoV-2

Room-temperature neutron and X-ray data collection of 3CL Mprofrom SARS-CoV-2

Protonation states in SARS-CoV-2 main protease mapped by neutron crystallography

Narrow Emission from Rb3Sb2I9 Nanoparticles

Contact Info

Product

Resources

About

Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Room-temperature neutron and X-ray data collection of 3CL M^profrom SARS-CoV-2

Narrow Emission from Rb₃Sb₂I₉ Nanoparticles