Quantifying X‐ray radiation damage in protein crystals at cryogenic temperatures
The dependence of radiation damage to protein crystals at cryogenic temperatures upon the X‐ray absorption cross‐section of the crystal has been examined. Lysozyme crystals containing varying heavy‐atom concentrations were irradiated and diffraction patterns were recorded as a function of the total...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2006-09, Vol.62 (9), p.1030-1038 |
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| container_end_page | 1038 |
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| container_issue | 9 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 62 |
| creator | Kmetko, Jan Husseini, Naji S. Naides, Matthew Kalinin, Yevgeniy Thorne, Robert E. |
| description | The dependence of radiation damage to protein crystals at cryogenic temperatures upon the X‐ray absorption cross‐section of the crystal has been examined. Lysozyme crystals containing varying heavy‐atom concentrations were irradiated and diffraction patterns were recorded as a function of the total number of incident photons. An experimental protocol and a coefficient of sensitivity to absorbed dose, proportional to the change in relative isotropic B factor, are defined that together yield a sensitive and robust measure of damage. Radiation damage per incident photon increases linearly with the absorption coefficient of the crystal, but damage per absorbed photon is the same for all heavy‐atom concentrations. Similar damage per absorbed photon is observed for crystals of three proteins with different molecular sizes and solvent contents. |
| doi_str_mv | 10.1107/S0907444906023869 |
| format | Article |
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Lysozyme crystals containing varying heavy‐atom concentrations were irradiated and diffraction patterns were recorded as a function of the total number of incident photons. An experimental protocol and a coefficient of sensitivity to absorbed dose, proportional to the change in relative isotropic B factor, are defined that together yield a sensitive and robust measure of damage. Radiation damage per incident photon increases linearly with the absorption coefficient of the crystal, but damage per absorbed photon is the same for all heavy‐atom concentrations. 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Section D, Biological crystallography.</title><addtitle>Acta Crystallogr D Biol Crystallogr</addtitle><description>The dependence of radiation damage to protein crystals at cryogenic temperatures upon the X‐ray absorption cross‐section of the crystal has been examined. Lysozyme crystals containing varying heavy‐atom concentrations were irradiated and diffraction patterns were recorded as a function of the total number of incident photons. An experimental protocol and a coefficient of sensitivity to absorbed dose, proportional to the change in relative isotropic B factor, are defined that together yield a sensitive and robust measure of damage. Radiation damage per incident photon increases linearly with the absorption coefficient of the crystal, but damage per absorbed photon is the same for all heavy‐atom concentrations. Similar damage per absorbed photon is observed for crystals of three proteins with different molecular sizes and solvent contents.</description><subject>Absorption</subject><subject>Cold Temperature</subject><subject>cryogenic temperatures</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Dose-Response Relationship, Radiation</subject><subject>Iodides - chemistry</subject><subject>Models, Statistical</subject><subject>Muramidase - chemistry</subject><subject>Photons</subject><subject>Proteins - chemistry</subject><subject>Proteins - radiation effects</subject><subject>radiation damage</subject><subject>Sensitivity and Specificity</subject><subject>Solvents - chemistry</subject><subject>Temperature</subject><subject>X-Ray Diffraction</subject><subject>X-Rays</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkNtKw0AYhBdRbK0-gDeyLxD9N8meLks9QkG0CvUq_NlDWWnSsEmR3PkIPqNPYksVBa9mYD4GZgg5ZXDOGMiLGWiQeZ5rEJBmSug9MmSZ1glALvf_-AE5attXAEjTTB6SARM61QzyIXl8WGPdBd-HekHnn-8fEXsa0QbswqqmFitcOBpq2sRV5zZqYt92uGwpdlu_Wrg6GNq5qnERu3V07TE58BvAnXzriDxfXz1NbpPp_c3dZDxNGqYUJEJYZnipJXfCO8edZF5rnpYI1lijvM2sLr1ROXrjlUDkqNFLLlLhWS6yETnb9TbrsnK2aGKoMPbFz7gNoHbAW1i6_jeHYvte8e-9YvxyOZtz4JB9ASveZQ0</recordid><startdate>200609</startdate><enddate>200609</enddate><creator>Kmetko, Jan</creator><creator>Husseini, Naji S.</creator><creator>Naides, Matthew</creator><creator>Kalinin, Yevgeniy</creator><creator>Thorne, Robert E.</creator><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>200609</creationdate><title>Quantifying X‐ray radiation damage in protein crystals at cryogenic temperatures</title><author>Kmetko, Jan ; Husseini, Naji S. ; Naides, Matthew ; Kalinin, Yevgeniy ; Thorne, Robert E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1880-66d1c5b975e6fee5e71f9952ba0dcdc8fd3d9bfc84afcf86aa5a9af75626f1463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Absorption</topic><topic>Cold Temperature</topic><topic>cryogenic temperatures</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Dose-Response Relationship, Radiation</topic><topic>Iodides - chemistry</topic><topic>Models, Statistical</topic><topic>Muramidase - chemistry</topic><topic>Photons</topic><topic>Proteins - chemistry</topic><topic>Proteins - radiation effects</topic><topic>radiation damage</topic><topic>Sensitivity and Specificity</topic><topic>Solvents - chemistry</topic><topic>Temperature</topic><topic>X-Ray Diffraction</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kmetko, Jan</creatorcontrib><creatorcontrib>Husseini, Naji S.</creatorcontrib><creatorcontrib>Naides, Matthew</creatorcontrib><creatorcontrib>Kalinin, Yevgeniy</creatorcontrib><creatorcontrib>Thorne, Robert E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Acta crystallographica. 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Lysozyme crystals containing varying heavy‐atom concentrations were irradiated and diffraction patterns were recorded as a function of the total number of incident photons. An experimental protocol and a coefficient of sensitivity to absorbed dose, proportional to the change in relative isotropic B factor, are defined that together yield a sensitive and robust measure of damage. Radiation damage per incident photon increases linearly with the absorption coefficient of the crystal, but damage per absorbed photon is the same for all heavy‐atom concentrations. Similar damage per absorbed photon is observed for crystals of three proteins with different molecular sizes and solvent contents.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Blackwell Publishing Ltd</pub><pmid>16929104</pmid><doi>10.1107/S0907444906023869</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1399-0047 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2006-09, Vol.62 (9), p.1030-1038 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Alma/SFX Local Collection |
| subjects | Absorption Cold Temperature cryogenic temperatures Crystallization Crystallography, X-Ray Dose-Response Relationship, Radiation Iodides - chemistry Models, Statistical Muramidase - chemistry Photons Proteins - chemistry Proteins - radiation effects radiation damage Sensitivity and Specificity Solvents - chemistry Temperature X-Ray Diffraction X-Rays |
| title | Quantifying X‐ray radiation damage in protein crystals at cryogenic temperatures |
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