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Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS
Three-dimensional structures derived from X-ray diffraction of protein crystals provide a wealth of information. Features and interactions important for the function of macromolecules can be deduced and catalytic mechanisms postulated. Still, many questions can remain, for example regarding metal ox...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004251/ https://www.ncbi.nlm.nih.gov/pubmed/21169688 http://dx.doi.org/10.1107/S0909049510033601 |
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author | Stoner-Ma, Deborah Skinner, John M. Schneider, Dieter K. Cowan, Matt Sweet, Robert M. Orville, Allen M. |
author_facet | Stoner-Ma, Deborah Skinner, John M. Schneider, Dieter K. Cowan, Matt Sweet, Robert M. Orville, Allen M. |
author_sort | Stoner-Ma, Deborah |
collection | PubMed |
description | Three-dimensional structures derived from X-ray diffraction of protein crystals provide a wealth of information. Features and interactions important for the function of macromolecules can be deduced and catalytic mechanisms postulated. Still, many questions can remain, for example regarding metal oxidation states and the interpretation of ‘mystery density’, i.e. ambiguous or unknown features within the electron density maps, especially at ∼2 Å resolutions typical of most macromolecular structures. Beamline X26-C at the National Synchrotron Light Source (NSLS), Brookhaven National Laboratory (BNL), provides researchers with the opportunity to not only determine the atomic structure of their samples but also to explore the electronic and vibrational characteristics of the sample before, during and after X-ray diffraction data collection. When samples are maintained under cryo-conditions, an opportunity to promote and follow photochemical reactions in situ as a function of X-ray exposure is also provided. Plans are in place to further expand the capabilities at beamline X26-C and to develop beamlines at NSLS-II, currently under construction at BNL, which will provide users access to a wide array of complementary spectroscopic methods in addition to high-quality X-ray diffraction data. |
format | Text |
id | pubmed-3004251 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-30042512010-12-23 Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS Stoner-Ma, Deborah Skinner, John M. Schneider, Dieter K. Cowan, Matt Sweet, Robert M. Orville, Allen M. J Synchrotron Radiat Diffraction Structural Biology Three-dimensional structures derived from X-ray diffraction of protein crystals provide a wealth of information. Features and interactions important for the function of macromolecules can be deduced and catalytic mechanisms postulated. Still, many questions can remain, for example regarding metal oxidation states and the interpretation of ‘mystery density’, i.e. ambiguous or unknown features within the electron density maps, especially at ∼2 Å resolutions typical of most macromolecular structures. Beamline X26-C at the National Synchrotron Light Source (NSLS), Brookhaven National Laboratory (BNL), provides researchers with the opportunity to not only determine the atomic structure of their samples but also to explore the electronic and vibrational characteristics of the sample before, during and after X-ray diffraction data collection. When samples are maintained under cryo-conditions, an opportunity to promote and follow photochemical reactions in situ as a function of X-ray exposure is also provided. Plans are in place to further expand the capabilities at beamline X26-C and to develop beamlines at NSLS-II, currently under construction at BNL, which will provide users access to a wide array of complementary spectroscopic methods in addition to high-quality X-ray diffraction data. International Union of Crystallography 2011-01-01 2010-11-05 /pmc/articles/PMC3004251/ /pubmed/21169688 http://dx.doi.org/10.1107/S0909049510033601 Text en © Deborah Stoner-Ma et al. 2011 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 Stoner-Ma, Deborah Skinner, John M. Schneider, Dieter K. Cowan, Matt Sweet, Robert M. Orville, Allen M. Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title | Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title_full | Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title_fullStr | Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title_full_unstemmed | Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title_short | Single-crystal Raman spectroscopy and X-ray crystallography at beamline X26-C of the NSLS |
title_sort | single-crystal raman spectroscopy and x-ray crystallography at beamline x26-c of the nsls |
topic | Diffraction Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004251/ https://www.ncbi.nlm.nih.gov/pubmed/21169688 http://dx.doi.org/10.1107/S0909049510033601 |
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