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Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography
A new detector system for protein crystallography is now being developed based on an X-ray HARP–FEA (high-gain avalanche rushing amorphous photoconductor–field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche...
Autores principales: | , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394816/ https://www.ncbi.nlm.nih.gov/pubmed/18421159 http://dx.doi.org/10.1107/S0909049508006584 |
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author | Miyoshi, Toshinobu Igarashi, Noriyuki Matsugaki, Naohiro Yamada, Yusuke Hirano, Keiichi Hyodo, Kazuyuki Tanioka, Kenkichi Egami, Norifumi Namba, Masakazu Kubota, Misao Kawai, Teruo Wakatsuki, Soichi |
author_facet | Miyoshi, Toshinobu Igarashi, Noriyuki Matsugaki, Naohiro Yamada, Yusuke Hirano, Keiichi Hyodo, Kazuyuki Tanioka, Kenkichi Egami, Norifumi Namba, Masakazu Kubota, Misao Kawai, Teruo Wakatsuki, Soichi |
author_sort | Miyoshi, Toshinobu |
collection | PubMed |
description | A new detector system for protein crystallography is now being developed based on an X-ray HARP–FEA (high-gain avalanche rushing amorphous photoconductor–field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche effect with a single driven FEA has several advantages over currently available area detectors, including higher sensitivity, higher spatial resolution and a higher frame rate. Preliminary evaluation of the detector has been carried out and its effectiveness has been confirmed. Next, diffraction images were measured with continuous rotation of a protein crystal, and the images were compared with those measured by the existing CCD detector; the system successfully obtained high-spatial-resolution images. Using shutterless measurement, the total measurement time can be reduced significantly, making the method appropriate for high-throughput protein crystallography. The X-ray HARP–FEA detector is an attractive candidate for the next generation of X-ray area detectors. |
format | Text |
id | pubmed-2394816 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-23948162009-03-05 Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography Miyoshi, Toshinobu Igarashi, Noriyuki Matsugaki, Naohiro Yamada, Yusuke Hirano, Keiichi Hyodo, Kazuyuki Tanioka, Kenkichi Egami, Norifumi Namba, Masakazu Kubota, Misao Kawai, Teruo Wakatsuki, Soichi J Synchrotron Radiat Diffraction Structural Biology A new detector system for protein crystallography is now being developed based on an X-ray HARP–FEA (high-gain avalanche rushing amorphous photoconductor–field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche effect with a single driven FEA has several advantages over currently available area detectors, including higher sensitivity, higher spatial resolution and a higher frame rate. Preliminary evaluation of the detector has been carried out and its effectiveness has been confirmed. Next, diffraction images were measured with continuous rotation of a protein crystal, and the images were compared with those measured by the existing CCD detector; the system successfully obtained high-spatial-resolution images. Using shutterless measurement, the total measurement time can be reduced significantly, making the method appropriate for high-throughput protein crystallography. The X-ray HARP–FEA detector is an attractive candidate for the next generation of X-ray area detectors. International Union of Crystallography 2008-05-01 2008-04-18 /pmc/articles/PMC2394816/ /pubmed/18421159 http://dx.doi.org/10.1107/S0909049508006584 Text en © International Union of Crystallography 2008 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Diffraction Structural Biology Miyoshi, Toshinobu Igarashi, Noriyuki Matsugaki, Naohiro Yamada, Yusuke Hirano, Keiichi Hyodo, Kazuyuki Tanioka, Kenkichi Egami, Norifumi Namba, Masakazu Kubota, Misao Kawai, Teruo Wakatsuki, Soichi Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title | Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title_full | Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title_fullStr | Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title_full_unstemmed | Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title_short | Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography |
title_sort | development of an x-ray harp–fea detector system for high-throughput protein crystallography |
topic | Diffraction Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394816/ https://www.ncbi.nlm.nih.gov/pubmed/18421159 http://dx.doi.org/10.1107/S0909049508006584 |
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