Non‐contact luminescence lifetime cryothermometry for macromolecular crystallography
Temperature is a very important parameter when aiming to minimize radiation damage to biological samples during experiments that utilize intense ionizing radiation. A novel technique for remote, non‐contact, in situ monitoring of the protein crystal temperature has been developed for the new I23 bea...
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| Veröffentlicht in: | Journal of synchrotron radiation 2017-05, Vol.24 (3), p.636-645 |
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| creator | Mykhaylyk, V. B. Wagner, A. Kraus, H. |
| description | Temperature is a very important parameter when aiming to minimize radiation damage to biological samples during experiments that utilize intense ionizing radiation. A novel technique for remote, non‐contact, in situ monitoring of the protein crystal temperature has been developed for the new I23 beamline at the Diamond Light Source, a facility dedicated to macromolecular crystallography (MX) with long‐wavelength X‐rays. The temperature is derived from the temperature‐dependent decay time constant of luminescence from a minuscule scintillation sensor ( |
| doi_str_mv | 10.1107/S1600577517003484 |
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The concept and practical implementation of a system for remote monitoring of the temperature of protein crystals down to 10 K using a microscopic bismuth germanate scintillation sensor are presented.</description><identifier>ISSN: 1600-5775</identifier><identifier>ISSN: 0909-0495</identifier><identifier>EISSN: 1600-5775</identifier><identifier>DOI: 10.1107/S1600577517003484</identifier><identifier>PMID: 28452755</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>bismuth germanate (BGO) ; cryogenic thermometry ; Crystals ; Decay ; Luminescence ; luminescence lifetime ; Particle physics ; protein crystalography ; Proteins ; Remote monitoring ; Research Papers ; Scintillation ; Sensors</subject><ispartof>Journal of synchrotron radiation, 2017-05, Vol.24 (3), p.636-645</ispartof><rights>V. B. Mykhaylyk et al. 2017</rights><rights>V. B. Mykhaylyk et al. 2017</rights><rights>V. B. Mykhaylyk et al. 2017 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5765-c352e850b9785181e4d1ffe150c26f0c9a31015c1fe7815919ad00e55c5d7c793</citedby><cites>FETCH-LOGICAL-c5765-c352e850b9785181e4d1ffe150c26f0c9a31015c1fe7815919ad00e55c5d7c793</cites><orcidid>0000-0001-8995-7324</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5477482/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5477482/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,11541,27901,27902,45550,45551,46027,46451,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28452755$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mykhaylyk, V. B.</creatorcontrib><creatorcontrib>Wagner, A.</creatorcontrib><creatorcontrib>Kraus, H.</creatorcontrib><title>Non‐contact luminescence lifetime cryothermometry for macromolecular crystallography</title><title>Journal of synchrotron radiation</title><addtitle>J Synchrotron Radiat</addtitle><description>Temperature is a very important parameter when aiming to minimize radiation damage to biological samples during experiments that utilize intense ionizing radiation. A novel technique for remote, non‐contact, in situ monitoring of the protein crystal temperature has been developed for the new I23 beamline at the Diamond Light Source, a facility dedicated to macromolecular crystallography (MX) with long‐wavelength X‐rays. The temperature is derived from the temperature‐dependent decay time constant of luminescence from a minuscule scintillation sensor (<0.05 mm3) located in very close proximity to the sample under test. In this work the underlying principle of cryogenic luminescence lifetime thermometry is presented, the features of the detection method and the choice of temperature sensor are discussed, and it is demonstrated how the temperature monitoring system was integrated within the viewing system of the endstation used for the visualization of protein crystals. The thermometry system was characterized using a Bi4Ge3O12 crystal scintillator that exhibits good responsivity of the decay time constant as a function of temperature over a wide range (8–270 K). The scintillation sensor was calibrated and the uncertainty of the temperature measurements over the primary operation temperature range of the beamline (30–150 K) was assessed to be ±1.6 K. It has been shown that the temperature of the sample holder, measured using the luminescence sensor, agrees well with the expected value. The technique was applied to characterize the thermal performance of different sample mounts that have been used in MX experiments at the I23 beamline. The thickness of the mount is shown to have the greatest impact upon the temperature distribution across the sample mount. Altogether, these tests and findings demonstrate the usefulness of the thermometry system in highlighting the challenges that remain to be addressed for the in‐vacuum MX experiment to become a reliable and indispensable tool for structural biology.
The concept and practical implementation of a system for remote monitoring of the temperature of protein crystals down to 10 K using a microscopic bismuth germanate scintillation sensor are presented.</description><subject>bismuth germanate (BGO)</subject><subject>cryogenic thermometry</subject><subject>Crystals</subject><subject>Decay</subject><subject>Luminescence</subject><subject>luminescence lifetime</subject><subject>Particle physics</subject><subject>protein crystalography</subject><subject>Proteins</subject><subject>Remote monitoring</subject><subject>Research Papers</subject><subject>Scintillation</subject><subject>Sensors</subject><issn>1600-5775</issn><issn>0909-0495</issn><issn>1600-5775</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNqFkc9u1DAQxi0Eon_gAbigSFy4LMw4mTi5IKGKFqoKDoWVOFmud9JNZceLnYBy6yPwjDwJXm1bFThwmtH4N5_m8yfEM4RXiKBen2MNQEoRKoCyaqoHYn87WmxnD-_1e-IgpSsArJUsH4s92VQkFdG-WH4Mw6_rnzYMo7Fj4SbfD5wsD5YL13c89p4LG-cwrjn64HmMc9GFWHhjY_DBsZ2ciVskjca5cBnNZj0_EY864xI_vamH4svxu89H7xdnn04-HL09W1hSNS1sSZIbgotWNYQNcrXCrmMksLLuwLamRECy2LFqkFpszQqAiSytlFVteSje7HQ304XnVb57jMbpTey9ibMOptd_vgz9Wl-G75oqpapGZoGXNwIxfJs4jdr32b5zZuAwJY0tVFIiSMjoi7_QqzDFIdvT2LRSKSBJmcIdlb8npcjd3TEIepua_ie1vPP8vou7jduYMtDugB-94_n_ivr0_KtcLglrKn8DIMmlVQ</recordid><startdate>201705</startdate><enddate>201705</enddate><creator>Mykhaylyk, V. B.</creator><creator>Wagner, A.</creator><creator>Kraus, H.</creator><general>International Union of Crystallography</general><general>John Wiley & Sons, Inc</general><scope>24P</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>JQ2</scope><scope>L7M</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8995-7324</orcidid></search><sort><creationdate>201705</creationdate><title>Non‐contact luminescence lifetime cryothermometry for macromolecular crystallography</title><author>Mykhaylyk, V. B. ; Wagner, A. ; Kraus, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5765-c352e850b9785181e4d1ffe150c26f0c9a31015c1fe7815919ad00e55c5d7c793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>bismuth germanate (BGO)</topic><topic>cryogenic thermometry</topic><topic>Crystals</topic><topic>Decay</topic><topic>Luminescence</topic><topic>luminescence lifetime</topic><topic>Particle physics</topic><topic>protein crystalography</topic><topic>Proteins</topic><topic>Remote monitoring</topic><topic>Research Papers</topic><topic>Scintillation</topic><topic>Sensors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mykhaylyk, V. B.</creatorcontrib><creatorcontrib>Wagner, A.</creatorcontrib><creatorcontrib>Kraus, H.</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of synchrotron radiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mykhaylyk, V. B.</au><au>Wagner, A.</au><au>Kraus, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Non‐contact luminescence lifetime cryothermometry for macromolecular crystallography</atitle><jtitle>Journal of synchrotron radiation</jtitle><addtitle>J Synchrotron Radiat</addtitle><date>2017-05</date><risdate>2017</risdate><volume>24</volume><issue>3</issue><spage>636</spage><epage>645</epage><pages>636-645</pages><issn>1600-5775</issn><issn>0909-0495</issn><eissn>1600-5775</eissn><abstract>Temperature is a very important parameter when aiming to minimize radiation damage to biological samples during experiments that utilize intense ionizing radiation. A novel technique for remote, non‐contact, in situ monitoring of the protein crystal temperature has been developed for the new I23 beamline at the Diamond Light Source, a facility dedicated to macromolecular crystallography (MX) with long‐wavelength X‐rays. The temperature is derived from the temperature‐dependent decay time constant of luminescence from a minuscule scintillation sensor (<0.05 mm3) located in very close proximity to the sample under test. In this work the underlying principle of cryogenic luminescence lifetime thermometry is presented, the features of the detection method and the choice of temperature sensor are discussed, and it is demonstrated how the temperature monitoring system was integrated within the viewing system of the endstation used for the visualization of protein crystals. The thermometry system was characterized using a Bi4Ge3O12 crystal scintillator that exhibits good responsivity of the decay time constant as a function of temperature over a wide range (8–270 K). The scintillation sensor was calibrated and the uncertainty of the temperature measurements over the primary operation temperature range of the beamline (30–150 K) was assessed to be ±1.6 K. It has been shown that the temperature of the sample holder, measured using the luminescence sensor, agrees well with the expected value. The technique was applied to characterize the thermal performance of different sample mounts that have been used in MX experiments at the I23 beamline. The thickness of the mount is shown to have the greatest impact upon the temperature distribution across the sample mount. Altogether, these tests and findings demonstrate the usefulness of the thermometry system in highlighting the challenges that remain to be addressed for the in‐vacuum MX experiment to become a reliable and indispensable tool for structural biology.
The concept and practical implementation of a system for remote monitoring of the temperature of protein crystals down to 10 K using a microscopic bismuth germanate scintillation sensor are presented.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>28452755</pmid><doi>10.1107/S1600577517003484</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-8995-7324</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | bismuth germanate (BGO) cryogenic thermometry Crystals Decay Luminescence luminescence lifetime Particle physics protein crystalography Proteins Remote monitoring Research Papers Scintillation Sensors |
| title | Non‐contact luminescence lifetime cryothermometry for macromolecular crystallography |
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