Langmuir-Blodgett nanotemplates for protein crystallography.
Identifieur interne : 000083 ( Main/Exploration ); précédent : 000082; suivant : 000084Langmuir-Blodgett nanotemplates for protein crystallography.
Auteurs : Eugenia Pechkova [Italie] ; Claudio Nicolini [Italie]Source :
- Nature protocols [ 1750-2799 ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Cholesterol side-chain cleavage enzyme (composition chimique), Conception d'appareillage (MeSH), Cristallisation (instrumentation), Cristallisation (méthodes), Cristallographie aux rayons X (instrumentation), Cristallographie aux rayons X (méthodes), Lysozyme (composition chimique), Marantaceae (composition chimique), Modèles moléculaires (MeSH), Nanostructures (composition chimique), Poulets (MeSH), Protéines (composition chimique), Protéines végétales (composition chimique).
- MESH :
- composition chimique : Cholesterol side-chain cleavage enzyme, Lysozyme, Marantaceae, Nanostructures, Protéines, Protéines végétales.
- méthodes : Cristallisation, Cristallographie aux rayons X.
- instrumentation : Animaux, Bovins, Conception d'appareillage, Cristallisation, Cristallographie aux rayons X, Modèles moléculaires, Poulets.
English descriptors
- KwdEn :
- Animals (MeSH), Cattle (MeSH), Chickens (MeSH), Cholesterol Side-Chain Cleavage Enzyme (chemistry), Crystallization (instrumentation), Crystallization (methods), Crystallography, X-Ray (instrumentation), Crystallography, X-Ray (methods), Equipment Design (MeSH), Marantaceae (chemistry), Models, Molecular (MeSH), Muramidase (chemistry), Nanostructures (chemistry), Plant Proteins (chemistry), Proteins (chemistry).
- MESH :
- chemical , chemistry : Cholesterol Side-Chain Cleavage Enzyme, Muramidase, Plant Proteins, Proteins.
- chemistry : Marantaceae, Nanostructures.
- instrumentation : Crystallization, Crystallography, X-Ray.
- methods : Crystallization, Crystallography, X-Ray.
- Animals, Cattle, Chickens, Equipment Design, Models, Molecular.
Abstract
The new generation of synchrotrons and microfocused beamlines has enabled great progress in X-ray protein crystallography, resulting in new 3D atomic structures for proteins of high interest to the pharmaceutical industry and life sciences. It is, however, often still challenging to produce protein crystals of sufficient size and quality (order, intensity of diffraction, radiation stability). In this protocol, we provide instructions for performing the Langmuir-Blodgett (LB) nanotemplate method, a crystallization approach that can be used for any protein (including membrane proteins). We describe how to produce highly ordered 2D LB protein monolayers at the air-water interface and deposit them on glass slides. LB-film formation can be observed by surface-pressure measurements and Brewster angle microscopy (BAM), although its quality can be characterized by atomic force microscopy (AFM) and nanogravimetry. Such films are then used as a 2D template for triggering 3D protein crystal formation by hanging-drop vapor diffusion. The procedure for forming the 2D template takes a few minutes. Structural information about the protein reorganization in the LB film during the crystallization process on the nano level can be obtained using an in situ submicron GISAXS (grazing-incidence small-angle X-ray scattering) method. MicroGISAXS spectra, measured directly at the interface of the LB films and protein solution in real time, as described in this protocol, can be interpreted in terms of the buildup of layers, islands, or holes. In our experience, the obtained LB crystals take 1-10 d to prepare and they are more ordered and radiation stable as compared with those produced using other crystallization methods.
DOI: 10.1038/nprot.2017.108
PubMed: 29189770
Affiliations:
Links toward previous steps (curation, corpus...)
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Nicolini, Pradalunga, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Fondazione EL.B.A. - Nicolini, Pradalunga</wicri:regionArea><wicri:noRegion>Pradalunga</wicri:noRegion></affiliation></author><author><name sortKey="Nicolini, Claudio" sort="Nicolini, Claudio" uniqKey="Nicolini C" first="Claudio" last="Nicolini">Claudio Nicolini</name><affiliation wicri:level="1"><nlm:affiliation>Laboratories of Biophysics and Nanotechnology, University of Genoa Medical School, Genoa, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Laboratories of Biophysics and Nanotechnology, University of Genoa Medical School, Genoa</wicri:regionArea><wicri:noRegion>Genoa</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Fondazione EL.B.A. - Nicolini, Pradalunga, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Fondazione EL.B.A. - Nicolini, Pradalunga</wicri:regionArea><wicri:noRegion>Pradalunga</wicri:noRegion></affiliation></author></analytic><series><title level="j">Nature protocols</title><idno type="eISSN">1750-2799</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cattle (MeSH)</term><term>Chickens (MeSH)</term><term>Cholesterol Side-Chain Cleavage Enzyme (chemistry)</term><term>Crystallization (instrumentation)</term><term>Crystallization (methods)</term><term>Crystallography, X-Ray (instrumentation)</term><term>Crystallography, X-Ray (methods)</term><term>Equipment Design (MeSH)</term><term>Marantaceae (chemistry)</term><term>Models, Molecular (MeSH)</term><term>Muramidase (chemistry)</term><term>Nanostructures (chemistry)</term><term>Plant Proteins (chemistry)</term><term>Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Cholesterol side-chain cleavage enzyme (composition chimique)</term><term>Conception d'appareillage (MeSH)</term><term>Cristallisation (instrumentation)</term><term>Cristallisation (méthodes)</term><term>Cristallographie aux rayons X (instrumentation)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Lysozyme (composition chimique)</term><term>Marantaceae (composition chimique)</term><term>Modèles moléculaires (MeSH)</term><term>Nanostructures (composition chimique)</term><term>Poulets (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines végétales (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cholesterol Side-Chain Cleavage Enzyme</term><term>Muramidase</term><term>Plant Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Marantaceae</term><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cholesterol side-chain cleavage enzyme</term><term>Lysozyme</term><term>Marantaceae</term><term>Nanostructures</term><term>Protéines</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Crystallization</term><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallization</term><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallisation</term><term>Cristallographie aux rayons X</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Chickens</term><term>Equipment Design</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Conception d'appareillage</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Poulets</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The new generation of synchrotrons and microfocused beamlines has enabled great progress in X-ray protein crystallography, resulting in new 3D atomic structures for proteins of high interest to the pharmaceutical industry and life sciences. It is, however, often still challenging to produce protein crystals of sufficient size and quality (order, intensity of diffraction, radiation stability). In this protocol, we provide instructions for performing the Langmuir-Blodgett (LB) nanotemplate method, a crystallization approach that can be used for any protein (including membrane proteins). We describe how to produce highly ordered 2D LB protein monolayers at the air-water interface and deposit them on glass slides. LB-film formation can be observed by surface-pressure measurements and Brewster angle microscopy (BAM), although its quality can be characterized by atomic force microscopy (AFM) and nanogravimetry. Such films are then used as a 2D template for triggering 3D protein crystal formation by hanging-drop vapor diffusion. The procedure for forming the 2D template takes a few minutes. Structural information about the protein reorganization in the LB film during the crystallization process on the nano level can be obtained using an in situ submicron GISAXS (grazing-incidence small-angle X-ray scattering) method. MicroGISAXS spectra, measured directly at the interface of the LB films and protein solution in real time, as described in this protocol, can be interpreted in terms of the buildup of layers, islands, or holes. In our experience, the obtained LB crystals take 1-10 d to prepare and they are more ordered and radiation stable as compared with those produced using other crystallization methods.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29189770</PMID><DateCompleted><Year>2017</Year><Month>12</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1750-2799</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>12</Issue><PubDate><Year>2017</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Nature protocols</Title><ISOAbbreviation>Nat Protoc</ISOAbbreviation></Journal><ArticleTitle>Langmuir-Blodgett nanotemplates for protein crystallography.</ArticleTitle><Pagination><MedlinePgn>2570-2589</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/nprot.2017.108</ELocationID><Abstract><AbstractText>The new generation of synchrotrons and microfocused beamlines has enabled great progress in X-ray protein crystallography, resulting in new 3D atomic structures for proteins of high interest to the pharmaceutical industry and life sciences. It is, however, often still challenging to produce protein crystals of sufficient size and quality (order, intensity of diffraction, radiation stability). In this protocol, we provide instructions for performing the Langmuir-Blodgett (LB) nanotemplate method, a crystallization approach that can be used for any protein (including membrane proteins). We describe how to produce highly ordered 2D LB protein monolayers at the air-water interface and deposit them on glass slides. LB-film formation can be observed by surface-pressure measurements and Brewster angle microscopy (BAM), although its quality can be characterized by atomic force microscopy (AFM) and nanogravimetry. Such films are then used as a 2D template for triggering 3D protein crystal formation by hanging-drop vapor diffusion. The procedure for forming the 2D template takes a few minutes. Structural information about the protein reorganization in the LB film during the crystallization process on the nano level can be obtained using an in situ submicron GISAXS (grazing-incidence small-angle X-ray scattering) method. MicroGISAXS spectra, measured directly at the interface of the LB films and protein solution in real time, as described in this protocol, can be interpreted in terms of the buildup of layers, islands, or holes. In our experience, the obtained LB crystals take 1-10 d to prepare and they are more ordered and radiation stable as compared with those produced using other crystallization methods.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pechkova</LastName><ForeName>Eugenia</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Laboratories of Biophysics and Nanotechnology, University of Genoa Medical School, Genoa, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Fondazione EL.B.A. - Nicolini, Pradalunga, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nicolini</LastName><ForeName>Claudio</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Laboratories of Biophysics and Nanotechnology, University of Genoa Medical School, Genoa, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Fondazione EL.B.A. - Nicolini, Pradalunga, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>11</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nat Protoc</MedlineTA><NlmUniqueID>101284307</NlmUniqueID><ISSNLinking>1750-2799</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.15.6</RegistryNumber><NameOfSubstance UI="D002786">Cholesterol Side-Chain Cleavage Enzyme</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.17</RegistryNumber><NameOfSubstance UI="D009113">Muramidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002645" MajorTopicYN="N">Chickens</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002786" MajorTopicYN="N">Cholesterol Side-Chain Cleavage Enzyme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="N">instrumentation</QualifierName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>12</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>12</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>12</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29189770</ArticleId><ArticleId IdType="pii">nprot.2017.108</ArticleId><ArticleId 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Pechkova</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|area= ThaumatinV1
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|texte= Langmuir-Blodgett nanotemplates for protein crystallography.
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