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Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors
The IBARAKI biological crystal diffractometer, iBIX, is a high-performance time-of-flight neutron single-crystal diffractometer for elucidating mainly the hydrogen, protonation and hydration structures of biological macromolecules in various life processes. Since the end of 2008, iBIX has been avail...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795571/ https://www.ncbi.nlm.nih.gov/pubmed/24121355 http://dx.doi.org/10.1107/S0909049513021845 |
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author | Kusaka, Katsuhiro Hosoya, Takaaki Yamada, Taro Tomoyori, Katsuaki Ohhara, Takashi Katagiri, Masaki Kurihara, Kazuo Tanaka, Ichiro Niimura, Nobuo |
author_facet | Kusaka, Katsuhiro Hosoya, Takaaki Yamada, Taro Tomoyori, Katsuaki Ohhara, Takashi Katagiri, Masaki Kurihara, Kazuo Tanaka, Ichiro Niimura, Nobuo |
author_sort | Kusaka, Katsuhiro |
collection | PubMed |
description | The IBARAKI biological crystal diffractometer, iBIX, is a high-performance time-of-flight neutron single-crystal diffractometer for elucidating mainly the hydrogen, protonation and hydration structures of biological macromolecules in various life processes. Since the end of 2008, iBIX has been available to users’ experiments supported by Ibaraki University. Since August 2012, an upgrade of the 14 existing detectors has begun and 16 new detectors have been installed for iBIX. The total measurement efficiency of the present diffractometer has been improved by one order of magnitude from the previous one with the increasing of accelerator power. In December 2012, commissioning of the new detectors was successful, and collection of the diffraction dataset of ribonucrease A as a standard protein was attempted in order to estimate the performance of the upgraded iBIX in comparison with previous results. The resolution of diffraction data, equivalence among intensities of symmetry-related reflections and reliability of the refined structure have been improved dramatically. iBIX is expected to be one of the highest-performance neutron single-crystal diffractometers for biological macromolecules in the world. |
format | Online Article Text |
id | pubmed-3795571 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-37955712013-10-15 Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors Kusaka, Katsuhiro Hosoya, Takaaki Yamada, Taro Tomoyori, Katsuaki Ohhara, Takashi Katagiri, Masaki Kurihara, Kazuo Tanaka, Ichiro Niimura, Nobuo J Synchrotron Radiat Diffraction Structural Biology The IBARAKI biological crystal diffractometer, iBIX, is a high-performance time-of-flight neutron single-crystal diffractometer for elucidating mainly the hydrogen, protonation and hydration structures of biological macromolecules in various life processes. Since the end of 2008, iBIX has been available to users’ experiments supported by Ibaraki University. Since August 2012, an upgrade of the 14 existing detectors has begun and 16 new detectors have been installed for iBIX. The total measurement efficiency of the present diffractometer has been improved by one order of magnitude from the previous one with the increasing of accelerator power. In December 2012, commissioning of the new detectors was successful, and collection of the diffraction dataset of ribonucrease A as a standard protein was attempted in order to estimate the performance of the upgraded iBIX in comparison with previous results. The resolution of diffraction data, equivalence among intensities of symmetry-related reflections and reliability of the refined structure have been improved dramatically. iBIX is expected to be one of the highest-performance neutron single-crystal diffractometers for biological macromolecules in the world. International Union of Crystallography 2013-11-01 2013-10-11 /pmc/articles/PMC3795571/ /pubmed/24121355 http://dx.doi.org/10.1107/S0909049513021845 Text en © Katsuhiro Kusaka et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Diffraction Structural Biology Kusaka, Katsuhiro Hosoya, Takaaki Yamada, Taro Tomoyori, Katsuaki Ohhara, Takashi Katagiri, Masaki Kurihara, Kazuo Tanaka, Ichiro Niimura, Nobuo Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title | Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title_full | Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title_fullStr | Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title_full_unstemmed | Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title_short | Evaluation of performance for IBARAKI biological crystal diffractometer iBIX with new detectors |
title_sort | evaluation of performance for ibaraki biological crystal diffractometer ibix with new detectors |
topic | Diffraction Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795571/ https://www.ncbi.nlm.nih.gov/pubmed/24121355 http://dx.doi.org/10.1107/S0909049513021845 |
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