ThaumatinV1, Main, Exploration, bibRecord, 000138

In vacuo X-ray data collection from graphene-wrapped protein crystals.

Identifieur interne : 000138 ( Main/Exploration ); précédent : 000137; suivant : 000139

In vacuo X-ray data collection from graphene-wrapped protein crystals.

Auteurs : Anna J. Warren [Royaume-Uni] ; Adam D. Crawshaw [Royaume-Uni] ; Jose Trincao [Royaume-Uni] ; Pierre Aller [Royaume-Uni] ; Simon Alcock [Royaume-Uni] ; Ioana Nistea [Royaume-Uni] ; Paula S. Salgado [Royaume-Uni] ; Gwyndaf Evans [Royaume-Uni]

Source :

Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2015.

RBID : pubmed:26457431

Descripteurs français

KwdFr :
- Aldose-ketose isomerases (composition chimique), Animaux (MeSH), Cristallisation (méthodes), Cristallographie aux rayons X (méthodes), Eau (composition chimique), Graphite (composition chimique), Lysozyme (composition chimique), Marantaceae (composition chimique), Poulets (MeSH), Protéines (composition chimique), Protéines végétales (composition chimique), Streptomyces (enzymologie), Température (MeSH), Vide (MeSH).
MESH :
- composition chimique : Aldose-ketose isomerases, Eau, Graphite, Lysozyme, Marantaceae, Protéines, Protéines végétales.
- enzymologie : Streptomyces.
- méthodes : Cristallisation, Cristallographie aux rayons X.
- Animaux, Poulets, Température, Vide.

English descriptors

KwdEn :
- Aldose-Ketose Isomerases (chemistry), Animals (MeSH), Chickens (MeSH), Crystallization (methods), Crystallography, X-Ray (methods), Graphite (chemistry), Marantaceae (chemistry), Muramidase (chemistry), Plant Proteins (chemistry), Proteins (chemistry), Streptomyces (enzymology), Temperature (MeSH), Vacuum (MeSH), Water (chemistry).
MESH :
- chemical , chemistry : Aldose-Ketose Isomerases, Graphite, Muramidase, Plant Proteins, Proteins, Water.
- chemistry : Marantaceae.
- enzymology : Streptomyces.
- methods : Crystallization, Crystallography, X-Ray.
- Animals, Chickens, Temperature, Vacuum.

Abstract

The measurement of diffraction data from macromolecular crystal samples held in vacuo holds the promise of a very low X-ray background and zero absorption of incident and scattered beams, leading to better data and the potential for accessing very long X-ray wavelengths (>3 Å) for native sulfur phasing. Maintaining the hydration of protein crystals under vacuum is achieved by the use of liquid jets, as with serial data collection at free-electron lasers, or is side-stepped by cryocooling the samples, as implemented at new synchrotron beamlines. Graphene has been shown to protect crystals from dehydration by creating an extremely thin layer that is impermeable to any exchanges with the environment. Furthermore, owing to its hydrophobicity, most of the aqueous solution surrounding the crystal is excluded during sample preparation, thus eliminating most of the background caused by liquid. Here, it is shown that high-quality data can be recorded at room temperature from graphene-wrapped protein crystals in a rough vacuum. Furthermore, it was observed that graphene protects crystals exposed to different relative humidities and a chemically harsh environment.

DOI: 10.1107/S1399004715014194
PubMed: 26457431
PubMed Central: PMC4601369

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000126
to stream Main, to step Curation: 000126

Le document en format XML

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<term>Chickens (MeSH)</term>
<term>Crystallization (methods)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Graphite (chemistry)</term>
<term>Marantaceae (chemistry)</term>
<term>Muramidase (chemistry)</term>
<term>Plant Proteins (chemistry)</term>
<term>Proteins (chemistry)</term>
<term>Streptomyces (enzymology)</term>
<term>Temperature (MeSH)</term>
<term>Vacuum (MeSH)</term>
<term>Water (chemistry)</term>
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<term>Cristallographie aux rayons X (méthodes)</term>
<term>Eau (composition chimique)</term>
<term>Graphite (composition chimique)</term>
<term>Lysozyme (composition chimique)</term>
<term>Marantaceae (composition chimique)</term>
<term>Poulets (MeSH)</term>
<term>Protéines (composition chimique)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Streptomyces (enzymologie)</term>
<term>Température (MeSH)</term>
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<term>Plant Proteins</term>
<term>Proteins</term>
<term>Water</term>
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<term>Eau</term>
<term>Graphite</term>
<term>Lysozyme</term>
<term>Marantaceae</term>
<term>Protéines</term>
<term>Protéines végétales</term>
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<term>Vacuum</term>
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<front><div type="abstract" xml:lang="en">The measurement of diffraction data from macromolecular crystal samples held in vacuo holds the promise of a very low X-ray background and zero absorption of incident and scattered beams, leading to better data and the potential for accessing very long X-ray wavelengths (>3 Å) for native sulfur phasing. Maintaining the hydration of protein crystals under vacuum is achieved by the use of liquid jets, as with serial data collection at free-electron lasers, or is side-stepped by cryocooling the samples, as implemented at new synchrotron beamlines. Graphene has been shown to protect crystals from dehydration by creating an extremely thin layer that is impermeable to any exchanges with the environment. Furthermore, owing to its hydrophobicity, most of the aqueous solution surrounding the crystal is excluded during sample preparation, thus eliminating most of the background caused by liquid. Here, it is shown that high-quality data can be recorded at room temperature from graphene-wrapped protein crystals in a rough vacuum. Furthermore, it was observed that graphene protects crystals exposed to different relative humidities and a chemically harsh environment.</div>
</front>
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<ArticleTitle>In vacuo X-ray data collection from graphene-wrapped protein crystals.</ArticleTitle>
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<Abstract><AbstractText>The measurement of diffraction data from macromolecular crystal samples held in vacuo holds the promise of a very low X-ray background and zero absorption of incident and scattered beams, leading to better data and the potential for accessing very long X-ray wavelengths (>3 Å) for native sulfur phasing. Maintaining the hydration of protein crystals under vacuum is achieved by the use of liquid jets, as with serial data collection at free-electron lasers, or is side-stepped by cryocooling the samples, as implemented at new synchrotron beamlines. Graphene has been shown to protect crystals from dehydration by creating an extremely thin layer that is impermeable to any exchanges with the environment. Furthermore, owing to its hydrophobicity, most of the aqueous solution surrounding the crystal is excluded during sample preparation, thus eliminating most of the background caused by liquid. Here, it is shown that high-quality data can be recorded at room temperature from graphene-wrapped protein crystals in a rough vacuum. Furthermore, it was observed that graphene protects crystals exposed to different relative humidities and a chemically harsh environment.</AbstractText>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Nistea</LastName>
<ForeName>Ioana</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, England.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Salgado</LastName>
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<Initials>PS</Initials>
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<ForeName>Gwyndaf</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, England.</Affiliation>
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<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011506">Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber>
<NameOfSubstance UI="C421864">hen egg lysozyme</NameOfSubstance>
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<NameOfSubstance UI="C023298">xylose isomerase</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D019747" MajorTopicYN="N">Aldose-Ketose Isomerases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002645" MajorTopicYN="N">Chickens</DescriptorName>
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<QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName>
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In vacuo X-ray data collection from graphene-wrapped protein crystals.

In vacuo X-ray data collection from graphene-wrapped protein crystals.

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