Time-resolved crystallography using the Hadamard transform.
Identifieur interne : 000159 ( Main/Exploration ); précédent : 000158; suivant : 000160Time-resolved crystallography using the Hadamard transform.
Auteurs : Briony A. Yorke [Royaume-Uni] ; Godfrey S. Beddard [Royaume-Uni] ; Robin L. Owen [Royaume-Uni] ; Arwen R. Pearson [Royaume-Uni]Source :
- Nature methods [ 1548-7105 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines végétales.
- méthodes : Cristallographie aux rayons X.
- Conformation des protéines, Facteurs temps, Rapport signal-bruit.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plant Proteins.
- methods : Crystallography, X-Ray.
- Protein Conformation, Signal-To-Noise Ratio, Time Factors.
Abstract
We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy.
DOI: 10.1038/nmeth.3139
PubMed: 25282611
PubMed Central: PMC4216935
Affiliations:
Links toward previous steps (curation, corpus...)
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Yorke</name><affiliation wicri:level="4"><nlm:affiliation>Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds</wicri:regionArea><orgName type="university">Université de Leeds</orgName><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName></affiliation></author><author><name sortKey="Beddard, Godfrey S" sort="Beddard, Godfrey S" uniqKey="Beddard G" first="Godfrey S" last="Beddard">Godfrey S. Beddard</name><affiliation wicri:level="4"><nlm:affiliation>School of Chemistry, The University of Leeds, Leeds, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Chemistry, The University of Leeds, Leeds</wicri:regionArea><orgName type="university">Université de Leeds</orgName><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName></affiliation></author><author><name sortKey="Owen, Robin L" sort="Owen, Robin L" uniqKey="Owen R" first="Robin L" last="Owen">Robin L. Owen</name><affiliation wicri:level="1"><nlm:affiliation>Diamond Light Source, Harwell Science and Innovation Campus, Didcot, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Diamond Light Source, Harwell Science and Innovation Campus, Didcot</wicri:regionArea><wicri:noRegion>Didcot</wicri:noRegion></affiliation></author><author><name sortKey="Pearson, Arwen R" sort="Pearson, Arwen R" uniqKey="Pearson A" first="Arwen R" last="Pearson">Arwen R. Pearson</name><affiliation wicri:level="4"><nlm:affiliation>Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds</wicri:regionArea><orgName type="university">Université de Leeds</orgName><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName></affiliation></author></analytic><series><title level="j">Nature methods</title><idno type="eISSN">1548-7105</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallography, X-Ray (methods)</term><term>Plant Proteins (chemistry)</term><term>Protein Conformation (MeSH)</term><term>Signal-To-Noise Ratio (MeSH)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Facteurs temps (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Rapport signal-bruit (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><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>Protein Conformation</term><term>Signal-To-Noise Ratio</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Facteurs temps</term><term>Rapport signal-bruit</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. 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This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yorke</LastName><ForeName>Briony A</ForeName><Initials>BA</Initials><AffiliationInfo><Affiliation>Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Beddard</LastName><ForeName>Godfrey S</ForeName><Initials>GS</Initials><AffiliationInfo><Affiliation>School of Chemistry, The University of Leeds, Leeds, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Owen</LastName><ForeName>Robin L</ForeName><Initials>RL</Initials><AffiliationInfo><Affiliation>Diamond Light Source, Harwell Science and Innovation Campus, Didcot, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pearson</LastName><ForeName>Arwen 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last="Yorke">Briony A. Yorke</name></region><name sortKey="Beddard, Godfrey S" sort="Beddard, Godfrey S" uniqKey="Beddard G" first="Godfrey S" last="Beddard">Godfrey S. Beddard</name><name sortKey="Owen, Robin L" sort="Owen, Robin L" uniqKey="Owen R" first="Robin L" last="Owen">Robin L. Owen</name><name sortKey="Pearson, Arwen R" sort="Pearson, Arwen R" uniqKey="Pearson A" first="Arwen R" last="Pearson">Arwen R. Pearson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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