Protein Layers And Their Use In Electron Microscopy
Protein layers (1) repeating regularly in two dimensions comprise protein protomers (2) which each comprise at least two monomers (5), (6) genetically fused together. The monomers (5), (6) are monomers of respective oligomer assemblies (3), (4) into which the monomers are assembled to assembly of th...
Gespeichert in:
Hauptverfasser: | , |
---|---|
Format: | Patent |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext bestellen |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | |
---|---|
container_issue | |
container_start_page | |
container_title | |
container_volume | |
creator | SINCLAIR JOHN CHARLES NOBLE MARTIN EDWARD MAENTYLAE |
description | Protein layers (1) repeating regularly in two dimensions comprise protein protomers (2) which each comprise at least two monomers (5), (6) genetically fused together. The monomers (5), (6) are monomers of respective oligomer assemblies (3), (4) into which the monomers are assembled to assembly of the protein layer. The first oligomer assembly (3) belongs to a dihedral point group of order O, where O equals (3), (4) or (6) and has a set of O rotational symmetry axes of order (2). The second oligomer assembly (4) has a rotational symmetry axis of order (2). Due to the symmetry of the oligomer assemblies (3), (4), the rotational symmetry axes of each second oligomer assembly (4) is aligned with one of said set of O rotational symmetry axes of a first oligomer assembly (3) with (2) protomers being arranged symmetrically therearound. Thus, an 2-fold fusion between the oligomer assemblies (3), (4) is produced and the arrangements of the rotational symmetry axes of the oligomer assemblies (3), (4) cause the protein layer to repeat regularly. The protein layer has many uses, for example to support molecular entities for biosensing, x-ray crystallography or electron microscopy. |
format | Patent |
fullrecord | <record><control><sourceid>epo_EVB</sourceid><recordid>TN_cdi_epo_espacenet_US2010202672A1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>US2010202672A1</sourcerecordid><originalsourceid>FETCH-epo_espacenet_US2010202672A13</originalsourceid><addsrcrecordid>eNrjZDAOKMovSc3MU_BJrEwtKlZwzEtRCMlIzSxSCC1OVfDMU3DNSU0uKcrPU_DNTC7KL07OL6jkYWBNS8wpTuWF0twMym6uIc4euqkF-fGpxQWJyal5qSXxocFGBoYGRgZGZuZGjobGxKkCAErhLII</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>patent</recordtype></control><display><type>patent</type><title>Protein Layers And Their Use In Electron Microscopy</title><source>esp@cenet</source><creator>SINCLAIR JOHN CHARLES ; NOBLE MARTIN EDWARD MAENTYLAE</creator><creatorcontrib>SINCLAIR JOHN CHARLES ; NOBLE MARTIN EDWARD MAENTYLAE</creatorcontrib><description>Protein layers (1) repeating regularly in two dimensions comprise protein protomers (2) which each comprise at least two monomers (5), (6) genetically fused together. The monomers (5), (6) are monomers of respective oligomer assemblies (3), (4) into which the monomers are assembled to assembly of the protein layer. The first oligomer assembly (3) belongs to a dihedral point group of order O, where O equals (3), (4) or (6) and has a set of O rotational symmetry axes of order (2). The second oligomer assembly (4) has a rotational symmetry axis of order (2). Due to the symmetry of the oligomer assemblies (3), (4), the rotational symmetry axes of each second oligomer assembly (4) is aligned with one of said set of O rotational symmetry axes of a first oligomer assembly (3) with (2) protomers being arranged symmetrically therearound. Thus, an 2-fold fusion between the oligomer assemblies (3), (4) is produced and the arrangements of the rotational symmetry axes of the oligomer assemblies (3), (4) cause the protein layer to repeat regularly. The protein layer has many uses, for example to support molecular entities for biosensing, x-ray crystallography or electron microscopy.</description><language>eng</language><subject>BEER ; BIOCHEMISTRY ; CALCULATING ; CHEMISTRY ; COMBINATORIAL CHEMISTRY ; COMPOSITIONS THEREOF ; COMPUTING ; COUNTING ; CULTURE MEDIA ; DERIVATIVES THEREOF ; ENZYMOLOGY ; HANDLING RECORD CARRIERS ; INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES ; LIBRARIES, e.g. CHEMICAL LIBRARIES, IN SILICOLIBRARIES ; MEASURING ; METALLURGY ; MICROBIOLOGY ; MICROORGANISMS OR ENZYMES ; MUTATION OR GENETIC ENGINEERING ; NUCLEIC ACIDS ; NUCLEOSIDES ; NUCLEOTIDES ; ORGANIC CHEMISTRY ; PEPTIDES ; PHYSICS ; PRESENTATION OF DATA ; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS ; RECOGNITION OF DATA ; RECORD CARRIERS ; SPIRITS ; SUGARS ; TESTING ; VINEGAR ; WINE</subject><creationdate>2010</creationdate><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://worldwide.espacenet.com/publicationDetails/biblio?FT=D&date=20100812&DB=EPODOC&CC=US&NR=2010202672A1$$EHTML$$P50$$Gepo$$Hfree_for_read</linktohtml><link.rule.ids>230,308,780,885,25563,76418</link.rule.ids><linktorsrc>$$Uhttps://worldwide.espacenet.com/publicationDetails/biblio?FT=D&date=20100812&DB=EPODOC&CC=US&NR=2010202672A1$$EView_record_in_European_Patent_Office$$FView_record_in_$$GEuropean_Patent_Office$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>SINCLAIR JOHN CHARLES</creatorcontrib><creatorcontrib>NOBLE MARTIN EDWARD MAENTYLAE</creatorcontrib><title>Protein Layers And Their Use In Electron Microscopy</title><description>Protein layers (1) repeating regularly in two dimensions comprise protein protomers (2) which each comprise at least two monomers (5), (6) genetically fused together. The monomers (5), (6) are monomers of respective oligomer assemblies (3), (4) into which the monomers are assembled to assembly of the protein layer. The first oligomer assembly (3) belongs to a dihedral point group of order O, where O equals (3), (4) or (6) and has a set of O rotational symmetry axes of order (2). The second oligomer assembly (4) has a rotational symmetry axis of order (2). Due to the symmetry of the oligomer assemblies (3), (4), the rotational symmetry axes of each second oligomer assembly (4) is aligned with one of said set of O rotational symmetry axes of a first oligomer assembly (3) with (2) protomers being arranged symmetrically therearound. Thus, an 2-fold fusion between the oligomer assemblies (3), (4) is produced and the arrangements of the rotational symmetry axes of the oligomer assemblies (3), (4) cause the protein layer to repeat regularly. The protein layer has many uses, for example to support molecular entities for biosensing, x-ray crystallography or electron microscopy.</description><subject>BEER</subject><subject>BIOCHEMISTRY</subject><subject>CALCULATING</subject><subject>CHEMISTRY</subject><subject>COMBINATORIAL CHEMISTRY</subject><subject>COMPOSITIONS THEREOF</subject><subject>COMPUTING</subject><subject>COUNTING</subject><subject>CULTURE MEDIA</subject><subject>DERIVATIVES THEREOF</subject><subject>ENZYMOLOGY</subject><subject>HANDLING RECORD CARRIERS</subject><subject>INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES</subject><subject>LIBRARIES, e.g. CHEMICAL LIBRARIES, IN SILICOLIBRARIES</subject><subject>MEASURING</subject><subject>METALLURGY</subject><subject>MICROBIOLOGY</subject><subject>MICROORGANISMS OR ENZYMES</subject><subject>MUTATION OR GENETIC ENGINEERING</subject><subject>NUCLEIC ACIDS</subject><subject>NUCLEOSIDES</subject><subject>NUCLEOTIDES</subject><subject>ORGANIC CHEMISTRY</subject><subject>PEPTIDES</subject><subject>PHYSICS</subject><subject>PRESENTATION OF DATA</subject><subject>PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS</subject><subject>RECOGNITION OF DATA</subject><subject>RECORD CARRIERS</subject><subject>SPIRITS</subject><subject>SUGARS</subject><subject>TESTING</subject><subject>VINEGAR</subject><subject>WINE</subject><fulltext>true</fulltext><rsrctype>patent</rsrctype><creationdate>2010</creationdate><recordtype>patent</recordtype><sourceid>EVB</sourceid><recordid>eNrjZDAOKMovSc3MU_BJrEwtKlZwzEtRCMlIzSxSCC1OVfDMU3DNSU0uKcrPU_DNTC7KL07OL6jkYWBNS8wpTuWF0twMym6uIc4euqkF-fGpxQWJyal5qSXxocFGBoYGRgZGZuZGjobGxKkCAErhLII</recordid><startdate>20100812</startdate><enddate>20100812</enddate><creator>SINCLAIR JOHN CHARLES</creator><creator>NOBLE MARTIN EDWARD MAENTYLAE</creator><scope>EVB</scope></search><sort><creationdate>20100812</creationdate><title>Protein Layers And Their Use In Electron Microscopy</title><author>SINCLAIR JOHN CHARLES ; NOBLE MARTIN EDWARD MAENTYLAE</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-epo_espacenet_US2010202672A13</frbrgroupid><rsrctype>patents</rsrctype><prefilter>patents</prefilter><language>eng</language><creationdate>2010</creationdate><topic>BEER</topic><topic>BIOCHEMISTRY</topic><topic>CALCULATING</topic><topic>CHEMISTRY</topic><topic>COMBINATORIAL CHEMISTRY</topic><topic>COMPOSITIONS THEREOF</topic><topic>COMPUTING</topic><topic>COUNTING</topic><topic>CULTURE MEDIA</topic><topic>DERIVATIVES THEREOF</topic><topic>ENZYMOLOGY</topic><topic>HANDLING RECORD CARRIERS</topic><topic>INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES</topic><topic>LIBRARIES, e.g. CHEMICAL LIBRARIES, IN SILICOLIBRARIES</topic><topic>MEASURING</topic><topic>METALLURGY</topic><topic>MICROBIOLOGY</topic><topic>MICROORGANISMS OR ENZYMES</topic><topic>MUTATION OR GENETIC ENGINEERING</topic><topic>NUCLEIC ACIDS</topic><topic>NUCLEOSIDES</topic><topic>NUCLEOTIDES</topic><topic>ORGANIC CHEMISTRY</topic><topic>PEPTIDES</topic><topic>PHYSICS</topic><topic>PRESENTATION OF DATA</topic><topic>PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS</topic><topic>RECOGNITION OF DATA</topic><topic>RECORD CARRIERS</topic><topic>SPIRITS</topic><topic>SUGARS</topic><topic>TESTING</topic><topic>VINEGAR</topic><topic>WINE</topic><toplevel>online_resources</toplevel><creatorcontrib>SINCLAIR JOHN CHARLES</creatorcontrib><creatorcontrib>NOBLE MARTIN EDWARD MAENTYLAE</creatorcontrib><collection>esp@cenet</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>SINCLAIR JOHN CHARLES</au><au>NOBLE MARTIN EDWARD MAENTYLAE</au><format>patent</format><genre>patent</genre><ristype>GEN</ristype><title>Protein Layers And Their Use In Electron Microscopy</title><date>2010-08-12</date><risdate>2010</risdate><abstract>Protein layers (1) repeating regularly in two dimensions comprise protein protomers (2) which each comprise at least two monomers (5), (6) genetically fused together. The monomers (5), (6) are monomers of respective oligomer assemblies (3), (4) into which the monomers are assembled to assembly of the protein layer. The first oligomer assembly (3) belongs to a dihedral point group of order O, where O equals (3), (4) or (6) and has a set of O rotational symmetry axes of order (2). The second oligomer assembly (4) has a rotational symmetry axis of order (2). Due to the symmetry of the oligomer assemblies (3), (4), the rotational symmetry axes of each second oligomer assembly (4) is aligned with one of said set of O rotational symmetry axes of a first oligomer assembly (3) with (2) protomers being arranged symmetrically therearound. Thus, an 2-fold fusion between the oligomer assemblies (3), (4) is produced and the arrangements of the rotational symmetry axes of the oligomer assemblies (3), (4) cause the protein layer to repeat regularly. The protein layer has many uses, for example to support molecular entities for biosensing, x-ray crystallography or electron microscopy.</abstract><oa>free_for_read</oa></addata></record> |
fulltext | fulltext_linktorsrc |
identifier | |
ispartof | |
issn | |
language | eng |
recordid | cdi_epo_espacenet_US2010202672A1 |
source | esp@cenet |
subjects | BEER BIOCHEMISTRY CALCULATING CHEMISTRY COMBINATORIAL CHEMISTRY COMPOSITIONS THEREOF COMPUTING COUNTING CULTURE MEDIA DERIVATIVES THEREOF ENZYMOLOGY HANDLING RECORD CARRIERS INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIRCHEMICAL OR PHYSICAL PROPERTIES LIBRARIES, e.g. CHEMICAL LIBRARIES, IN SILICOLIBRARIES MEASURING METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING NUCLEIC ACIDS NUCLEOSIDES NUCLEOTIDES ORGANIC CHEMISTRY PEPTIDES PHYSICS PRESENTATION OF DATA PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS RECOGNITION OF DATA RECORD CARRIERS SPIRITS SUGARS TESTING VINEGAR WINE |
title | Protein Layers And Their Use In Electron Microscopy |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T11%3A58%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-epo_EVB&rft_val_fmt=info:ofi/fmt:kev:mtx:patent&rft.genre=patent&rft.au=SINCLAIR%20JOHN%20CHARLES&rft.date=2010-08-12&rft_id=info:doi/&rft_dat=%3Cepo_EVB%3EUS2010202672A1%3C/epo_EVB%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |