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Improvement of an automated protein crystal exchange system PAM for high-throughput data collection

Photon Factory Automated Mounting system (PAM) protein crystal exchange systems are available at the following Photon Factory macromolecular beamlines: BL-1A, BL-5A, BL-17A, AR-NW12A and AR-NE3A. The beamline AR-NE3A has been constructed for high-throughput macromolecular crystallography and is dedi...

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Autores principales: Hiraki, Masahiko, Yamada, Yusuke, Chavas, Leonard M. G., Wakatsuki, Soichi, Matsugaki, Naohiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795550/
https://www.ncbi.nlm.nih.gov/pubmed/24121334
http://dx.doi.org/10.1107/S0909049513021067
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author Hiraki, Masahiko
Yamada, Yusuke
Chavas, Leonard M. G.
Wakatsuki, Soichi
Matsugaki, Naohiro
author_facet Hiraki, Masahiko
Yamada, Yusuke
Chavas, Leonard M. G.
Wakatsuki, Soichi
Matsugaki, Naohiro
author_sort Hiraki, Masahiko
collection PubMed
description Photon Factory Automated Mounting system (PAM) protein crystal exchange systems are available at the following Photon Factory macromolecular beamlines: BL-1A, BL-5A, BL-17A, AR-NW12A and AR-NE3A. The beamline AR-NE3A has been constructed for high-throughput macromolecular crystallography and is dedicated to structure-based drug design. The PAM liquid-nitrogen Dewar can store a maximum of three SSRL cassettes. Therefore, users have to interrupt their experiments and replace the cassettes when using four or more of them during their beam time. As a result of investigation, four or more cassettes were used in AR-NE3A alone. For continuous automated data collection, the size of the liquid-nitrogen Dewar for the AR-NE3A PAM was increased, doubling the capacity. In order to check the calibration with the new Dewar and the cassette stand, calibration experiments were repeatedly performed. Compared with the current system, the parameters of the novel system are shown to be stable.
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spelling pubmed-37955502013-10-15 Improvement of an automated protein crystal exchange system PAM for high-throughput data collection Hiraki, Masahiko Yamada, Yusuke Chavas, Leonard M. G. Wakatsuki, Soichi Matsugaki, Naohiro J Synchrotron Radiat Diffraction Structural Biology Photon Factory Automated Mounting system (PAM) protein crystal exchange systems are available at the following Photon Factory macromolecular beamlines: BL-1A, BL-5A, BL-17A, AR-NW12A and AR-NE3A. The beamline AR-NE3A has been constructed for high-throughput macromolecular crystallography and is dedicated to structure-based drug design. The PAM liquid-nitrogen Dewar can store a maximum of three SSRL cassettes. Therefore, users have to interrupt their experiments and replace the cassettes when using four or more of them during their beam time. As a result of investigation, four or more cassettes were used in AR-NE3A alone. For continuous automated data collection, the size of the liquid-nitrogen Dewar for the AR-NE3A PAM was increased, doubling the capacity. In order to check the calibration with the new Dewar and the cassette stand, calibration experiments were repeatedly performed. Compared with the current system, the parameters of the novel system are shown to be stable. International Union of Crystallography 2013-11-01 2013-10-01 /pmc/articles/PMC3795550/ /pubmed/24121334 http://dx.doi.org/10.1107/S0909049513021067 Text en © Masahiko Hiraki 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
Hiraki, Masahiko
Yamada, Yusuke
Chavas, Leonard M. G.
Wakatsuki, Soichi
Matsugaki, Naohiro
Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title_full Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title_fullStr Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title_full_unstemmed Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title_short Improvement of an automated protein crystal exchange system PAM for high-throughput data collection
title_sort improvement of an automated protein crystal exchange system pam for high-throughput data collection
topic Diffraction Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795550/
https://www.ncbi.nlm.nih.gov/pubmed/24121334
http://dx.doi.org/10.1107/S0909049513021067
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