Radiation decay of thaumatin crystals at three X-ray energies.
Identifieur interne : 000130 ( Main/Exploration ); précédent : 000129; suivant : 000131Radiation decay of thaumatin crystals at three X-ray energies.
Auteurs : Dorothee Liebschner [Japon] ; Gerold Rosenbaum [États-Unis] ; Miroslawa Dauter [États-Unis] ; Zbigniew Dauter [États-Unis]Source :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Plantes, Protéines végétales.
- méthodes : Cristallographie aux rayons X.
- Cristallisation.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins.
- chemistry : Plants.
- methods : Crystallography, X-Ray.
- Crystallization.
Abstract
Radiation damage is an unavoidable obstacle in X-ray crystallographic data collection for macromolecular structure determination, so it is important to know how much radiation a sample can endure before being degraded beyond an acceptable limit. In the literature, the threshold at which the average intensity of all recorded reflections decreases to a certain fraction of the initial value is called the `dose limit'. The first estimated D50 dose-limit value, at which the average diffracted intensity was reduced to 50%, was 20 MGy and was derived from observing sample decay in electron-diffraction experiments. A later X-ray study carried out at 100 K on ferritin protein crystals arrived at a D50 of 43 MGy, and recommended an intensity reduction of protein reflections to 70%, D70, corresponding to an absorbed dose of 30 MGy, as a more appropriate limit for macromolecular crystallography. In the macromolecular crystallography community, the rate of intensity decay with dose was then assumed to be similar for all protein crystals. A series of diffraction images of cryocooled (100 K) thaumatin crystals at identical small, 2° rotation intervals were recorded at X-ray energies of 6.33 , 12.66 and 19.00 keV. Five crystals were used for each wavelength. The decay in the average diffraction intensity to 70% of the initial value, for data extending to 2.45 Å resolution, was determined to be about 7.5 MGy at 6.33 keV and about 11 MGy at the two higher energies.
DOI: 10.1107/S1399004715001030
PubMed: 25849388
PubMed Central: PMC4388262
Affiliations:
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Organization, Tsukuba</wicri:regionArea><wicri:noRegion>Tsukuba</wicri:noRegion></affiliation></author><author><name sortKey="Rosenbaum, Gerold" sort="Rosenbaum, Gerold" uniqKey="Rosenbaum G" first="Gerold" last="Rosenbaum">Gerold Rosenbaum</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry, University of Georgia and Structural Biology Center, Argonne National Laboratory, Argonne, IL 60439, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Georgia and Structural Biology Center, Argonne National Laboratory, Argonne, IL 60439</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author><author><name sortKey="Dauter, Miroslawa" sort="Dauter, Miroslawa" uniqKey="Dauter M" first="Miroslawa" last="Dauter">Miroslawa Dauter</name><affiliation wicri:level="2"><nlm:affiliation>Leidos Biomedical Research Inc., Basic Science Program, Argonne National Laboratory, Argonne, IL 60439, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Leidos Biomedical Research Inc., Basic Science Program, Argonne National Laboratory, Argonne, IL 60439</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author><author><name sortKey="Dauter, Zbigniew" sort="Dauter, Zbigniew" uniqKey="Dauter Z" first="Zbigniew" last="Dauter">Zbigniew Dauter</name><affiliation wicri:level="2"><nlm:affiliation>Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="eISSN">1399-0047</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (MeSH)</term><term>Crystallography, X-Ray (methods)</term><term>Plant Proteins (chemistry)</term><term>Plants (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Plantes (composition chimique)</term><term>Protéines végétales (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Plantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallisation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Radiation damage is an unavoidable obstacle in X-ray crystallographic data collection for macromolecular structure determination, so it is important to know how much radiation a sample can endure before being degraded beyond an acceptable limit. In the literature, the threshold at which the average intensity of all recorded reflections decreases to a certain fraction of the initial value is called the `dose limit'. The first estimated D50 dose-limit value, at which the average diffracted intensity was reduced to 50%, was 20 MGy and was derived from observing sample decay in electron-diffraction experiments. A later X-ray study carried out at 100 K on ferritin protein crystals arrived at a D50 of 43 MGy, and recommended an intensity reduction of protein reflections to 70%, D70, corresponding to an absorbed dose of 30 MGy, as a more appropriate limit for macromolecular crystallography. In the macromolecular crystallography community, the rate of intensity decay with dose was then assumed to be similar for all protein crystals. A series of diffraction images of cryocooled (100 K) thaumatin crystals at identical small, 2° rotation intervals were recorded at X-ray energies of 6.33 , 12.66 and 19.00 keV. Five crystals were used for each wavelength. The decay in the average diffraction intensity to 70% of the initial value, for data extending to 2.45 Å resolution, was determined to be about 7.5 MGy at 6.33 keV and about 11 MGy at the two higher energies. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25849388</PMID><DateCompleted><Year>2016</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>71</Volume><Issue>Pt 4</Issue><PubDate><Year>2015</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Radiation decay of thaumatin crystals at three X-ray energies.</ArticleTitle><Pagination><MedlinePgn>772-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S1399004715001030</ELocationID><Abstract><AbstractText>Radiation damage is an unavoidable obstacle in X-ray crystallographic data collection for macromolecular structure determination, so it is important to know how much radiation a sample can endure before being degraded beyond an acceptable limit. In the literature, the threshold at which the average intensity of all recorded reflections decreases to a certain fraction of the initial value is called the `dose limit'. The first estimated D50 dose-limit value, at which the average diffracted intensity was reduced to 50%, was 20 MGy and was derived from observing sample decay in electron-diffraction experiments. A later X-ray study carried out at 100 K on ferritin protein crystals arrived at a D50 of 43 MGy, and recommended an intensity reduction of protein reflections to 70%, D70, corresponding to an absorbed dose of 30 MGy, as a more appropriate limit for macromolecular crystallography. In the macromolecular crystallography community, the rate of intensity decay with dose was then assumed to be similar for all protein crystals. A series of diffraction images of cryocooled (100 K) thaumatin crystals at identical small, 2° rotation intervals were recorded at X-ray energies of 6.33 , 12.66 and 19.00 keV. Five crystals were used for each wavelength. The decay in the average diffraction intensity to 70% of the initial value, for data extending to 2.45 Å resolution, was determined to be about 7.5 MGy at 6.33 keV and about 11 MGy at the two higher energies. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liebschner</LastName><ForeName>Dorothee</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization, Tsukuba, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rosenbaum</LastName><ForeName>Gerold</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Georgia and Structural Biology Center, Argonne National Laboratory, Argonne, IL 60439, USA.</Affiliation></AffiliationInfo></Author><Author 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last="Liebschner">Dorothee Liebschner</name></noRegion></country><country name="États-Unis"><region name="Illinois"><name sortKey="Rosenbaum, Gerold" sort="Rosenbaum, Gerold" uniqKey="Rosenbaum G" first="Gerold" last="Rosenbaum">Gerold Rosenbaum</name></region><name sortKey="Dauter, Miroslawa" sort="Dauter, Miroslawa" uniqKey="Dauter M" first="Miroslawa" last="Dauter">Miroslawa Dauter</name><name sortKey="Dauter, Zbigniew" sort="Dauter, Zbigniew" uniqKey="Dauter Z" first="Zbigniew" last="Dauter">Zbigniew Dauter</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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