An upgraded neutron diffractometer (BIX-IM) for macromolecules with a neutron imaging plate

A high-performance neutron diffractometer for biological crystallography (BIX-3) has been constructed at JRR-3M in the Japan Atomic Energy Research Institute (JAERI) in order to determine the hydrogen-atom positions in biological macromolecules. It uses several recent technical innovations, such as a neutron imaging plate and an elastically bent silicon monochromator developed by the authors. These have made it possible to realise a compact vertical arrangement of the diffractometer. Diffraction data have been collected from the proteins rubredoxin and myoglobin in about one month, to a resolution of 1.5 Å. The data were good enough to identify the hydrogen atoms with high accuracy. By adopting a crystal-step scan method for measuring Bragg diffraction intensities, the signal-to-noise ratio was much better than that of the Laue method. This shows that BIX-3 is one of the best-performing machines for neutron protein crystallography in the world today.

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High resolution neutron protein crystallography. Hydrogen and hydration in proteins

Zeitschrift für Kristallographie - Crystalline Materials ◽

10.1524/zkri.218.2.96.20666 ◽

2003 ◽

Vol 218 (2) ◽

Cited By ~ 7

Author(s):

N. Niimura ◽

T. Chatake ◽

A. Ostermann ◽

K. Kurihara ◽

I. Tanaka

Keyword(s):

High Resolution ◽

Dynamical Behavior ◽

Protein Crystallography ◽

Neutron Imaging ◽

Imaging Plate ◽

Biological Macromolecules ◽

Hydrogen Atoms ◽

Neutron Diffractometer ◽

Neutron Protein Crystallography ◽

Acidic Hydrogen

AbstractNeutron diffraction provides an experimental method of directly locating hydrogen atoms in proteins, and the development of the neutron imaging plate (NIP) became a breakthrough event in neutron protein crystallography. The general features of the NIP are reviewed. A high resolution neutron diffractometer dedicated to biological macromolecules (BIX-3) with the NIP has been constructed at Japan Atomic Energy Research Institute and this has enabled 1.5 Å resolution structural analyses of several proteins to be carried out. The specifications of BIX-3 and LADI (a quasi-Laue type diffractometer installed in the Institut Laue-Langevin) are compared. The crystal structures of myoglobin, wild type rubredoxin and a mutant of rubredoxin have been carried out using BIX-3. From these studies, several topics, such as the location of hydrogen bonds and certain acidic hydrogen atoms, the identification of methyl hydrogen atoms, details of H/D exchange and dynamical behavior of hydration structures have been investigated, and important information has been extracted from the structural results. Finally, a systematic procedure to grow large single crystals of proteins or nucleic acids is described.

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BioDiff - a neutron diffractometer for protein crystallography

Acta Crystallographica Section A Foundations and Advances ◽

10.1107/s2053273314087841 ◽

2014 ◽

Vol 70 (a1) ◽

pp. C1215-C1215

Author(s):

Tobias Schrader ◽

Andreas Ostermann ◽

Michael Monkenbusch ◽

Bernhard Laatsch ◽

Philipp Jüttner ◽

...

Keyword(s):

Neutron Beam ◽

Pyrolytic Graphite ◽

Ccd Camera ◽

Background Level ◽

Neutron Imaging ◽

Imaging Plate ◽

Active Centre ◽

Joint Project ◽

Neutron Diffractometer

The research reactor Heinz Maier-Leibnitz (FRM II) is a modern high flux neutron source which feeds some 30 state of the art neutron beam instruments. Currently 24 are operational, others in commissioning or under construction. The newly built neutron single crystal diffractometer BIODIFF is especially designed to collect data from crystals with large unit cells. The main field of application is the structural analysis of proteins, especially the determination of hydrogen atom positions. BIODIFF is a joint project of the Jülich Centre for Neutron Science (JCNS) and the FRM II. Typical scientific questions addressed are the determination of protonation states of amino acid side chains (see e. g. [1,2]) and the characterization of the hydrogen bonding network between the protein active centre and an inhibitor or substrate. BIODIFF is designed as a monochromatic instrument. By using a highly orientated pyrolytic graphite monochromator (PG002) the diffractometer is able to operate in the wavelength range of 2.4 Å to about 5.6 Å. Contaminations of higher order wavelengths are removed by a neutron velocity selector. To cover a large solid angle the main detector of BIODIFF consists of a neutron imaging plate in a cylindrical geometry with online read-out capability. A fast Li/ZnS scintillator CCD camera is available for additional detection abilities. An optical CCD-camera pointing at the sample position is used to quickly align the crystal with respect to the neutron beam. The main advantage of BIODIFF is the possibility to adapt the wavelength to the size of the unit cell of the sample crystal while operating with a clean monochromatic beam that keeps the background level low. BIODIFF is equipped with a standard Oxford Cryosystem "Cryostream 700+" which allows measurements in the temperature regime from 90 K up to 500 K (see Figure underneath).

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Neutron Diffractometer for Bio-Crystallography (BIX) with an Imaging Plate Neutron Detector

Neutrons in Biology ◽

10.1007/978-1-4615-5847-7_35 ◽

1996 ◽

pp. 415-422

Author(s):

Nobuo Niimura

Keyword(s):

Neutron Detector ◽

Imaging Plate ◽

Neutron Diffractometer

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The character and application of a neutron imaging plate (NIP)

Physica B Condensed Matter ◽

10.1016/s0921-4526(97)00532-2 ◽

1997 ◽

Vol 241-243 ◽

pp. 139-141 ◽

Cited By ~ 5

Author(s):

Y Karasawa ◽

S Kumazawa ◽

N Miimura

Keyword(s):

Neutron Imaging ◽

Imaging Plate

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2-D Evaluation of Bred Tritium Using Neutron Imaging Plate

IEEE Transactions on Plasma Science ◽

10.1109/tps.2019.2955497 ◽

2020 ◽

Vol 48 (6) ◽

pp. 1831-1835

Author(s):

K. Mukai ◽

Y. Ogino ◽

J. Yagi ◽

S. Konishi

Keyword(s):

Neutron Imaging ◽

Imaging Plate

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Gamma-ray sensitivity and shielding of a neutron imaging plate

Journal of Applied Crystallography ◽

10.1107/s0021889899005701 ◽

1999 ◽

Vol 32 (5) ◽

pp. 878-882 ◽

Cited By ~ 14

Author(s):

Y. Karasawa Haga ◽

S. Kumazawa ◽

N. Niimura

Keyword(s):

Thermal Neutron ◽

Energy Dependence ◽

Gamma Rays ◽

Gamma Ray ◽

Neutron Imaging ◽

Atomic Energy ◽

Imaging Plate ◽

Energy Research ◽

Experimental Hall ◽

Lead Foil

The energy dependence of gamma-ray sensitivity of a neutron imaging plate (NIP) has been measured. The gamma-ray sensitivity is equivalent to one half that of a thermal neutron at a gamma-ray energy less than 300 keV, and 1/40 at greater than 300 keV. The shielding of the NIP, by lead, from gamma rays in the experimental hall of the reactor JRR-3M of the Japan Atomic Energy Research Institute (JAERI) was measured. It was found that lead of thickness 40 mm is sufficient to reduce the gamma-ray background to 1/10 on a normalized scale. Covering the NIP with lead foil of thickness 1 mm results in a decrease of the gamma-ray background without reduction of the neutron signal.

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Performance assessment of imaging plates for the JHR transfer Neutron Imaging System

EPJ Web of Conferences ◽

10.1051/epjconf/201817004021 ◽

2018 ◽

Vol 170 ◽

pp. 04021

Author(s):

E. Simon ◽

P. Guimbal

Keyword(s):

Performance Assessment ◽

Dynamic Range ◽

Imaging System ◽

Computed Radiography ◽

High Sensitivity ◽

High Dynamic Range ◽

Neutron Imaging ◽

Imaging Plate ◽

Intimate Contact ◽

Imaging Plates

The underwater Neutron Imaging System to be installed in the Jules Horowitz Reactor (JHR-NIS) is based on a transfer method using a neutron activated beta-emitter like Dysprosium. The information stored in the converter is to be offline transferred on a specific imaging system, still to be defined. Solutions are currently under investigation for the JHR-NIS in order to anticipate the disappearance of radiographic films commonly used in these applications. We report here the performance assessment of Computed Radiography imagers (Imaging Plates) performed at LLB/Orphée (CEA Saclay). Several imaging plate types are studied, in one hand in the configuration involving an intimate contact with an activated dysprosium foil converter: Fuji BAS-TR, Fuji UR-1 and Carestream Flex XL Blue imaging plates, and in the other hand by using a prototypal imaging plate doped with dysprosium and thus not needing any contact with a separate converter foil. The results for these imaging plates are compared with those obtained with gadolinium doped imaging plate used in direct neutron imaging (Fuji BAS-ND). The detection performances of the different imagers are compared regarding resolution and noise. The many advantages of using imaging plates over radiographic films (high sensitivity, linear response, high dynamic range) could palliate its lower intrinsic resolution.

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An imaging-plate detector for small-angle neutron scattering

Journal of Applied Crystallography ◽

10.1107/s0021889800009067 ◽

2000 ◽

Vol 33 (5) ◽

pp. 1253-1261 ◽

Cited By ~ 5

Author(s):

Y. T. Cheng ◽

D. F. R. Mildner ◽

H. H. Chen-Mayer ◽

V. A. Sharov ◽

C. J. Glinka

Keyword(s):

Neutron Scattering ◽

Small Angle ◽

Small Angle Neutron Scattering ◽

Imaging Techniques ◽

Neutron Imaging ◽

Small Samples ◽

Imaging Plate ◽

Position Sensitive ◽

Transfer Method ◽

Imaging Plates

Small-angle neutron scattering (SANS) measurements have been performed on long-flight-path pinhole-collimation SANS instruments using, as a two-dimensional position-sensitive detector, both a neutron imaging plate, incorporating gadolinium, and a two-step transfer method, with dysprosium foil as the image transfer medium. The measurements are compared with corresponding data taken using conventional position-sensitive gas proportional counters on the SANS instruments in order to assess the viability of the imaging techniques. The imaging plates have pixel sizes of about two orders of magnitude smaller than those of the gas proportional counter. The reduced pixel size provides definite advantages over the gas counter in certain specific situations, namely when limited space necessitates a short sample-to-detector distance, when only small samples (comparable in size to the detector pixels) are available, or when used in conjunction with focusing beam optics.

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