About: Optimization of the crystallizability of a single-chain antibody fragment

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1107/S2053230X1402247X
Description	Single-chain variable antibody fragments (scFvs) are molecules with immense therapeutic and diagnostic potential. Knowledge of their three-dimensional structure is important for understanding their antigen-binding mode as well as for protein-engineering approaches such as antibody humanization. A major obstacle to the crystallization of single-chain variable antibody fragments is their relatively poor homogeneity caused by spontaneous oligomerization. A new approach to optimization of the crystallizability of single-chain variable antibody fragments is demonstrated using a representative single-chain variable fragment derived from the anti-CD3 antibody MEM-57. A Thermofluor-based assay was utilized to screen for optimal conditions for antibody-fragment stability and homogeneity. Such an optimization of the protein storage buffer led to a significantly improved ability of the scFv MEM-57 to yield crystals. Single-chain variable antibody fragments (scFvs) are molecules with immense therapeutic and diagnostic potential. Knowledge of their three-dimensional structure is important for understanding their antigen-binding mode as well as for protein-engineering approaches such as antibody humanization. A major obstacle to the crystallization of single-chain variable antibody fragments is their relatively poor homogeneity caused by spontaneous oligomerization. A new approach to optimization of the crystallizability of single-chain variable antibody fragments is demonstrated using a representative single-chain variable fragment derived from the anti-CD3 antibody MEM-57. A Thermofluor-based assay was utilized to screen for optimal conditions for antibody-fragment stability and homogeneity. Such an optimization of the protein storage buffer led to a significantly improved ability of the scFv MEM-57 to yield crystals. (en)
Title	Optimization of the crystallizability of a single-chain antibody fragment Optimization of the crystallizability of a single-chain antibody fragment (en)
skos:prefLabel	Optimization of the crystallizability of a single-chain antibody fragment Optimization of the crystallizability of a single-chain antibody fragment (en)
skos:notation	RIV/00216208:11310/14:10289033!RIV15-MSM-11310___
http://linked.open...avai/riv/aktivita	I P S
http://linked.open...avai/riv/aktivity	I, P(LK11205), S
http://linked.open...iv/cisloPeriodika	December 2014
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Škerlová, Jana
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	34984
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/14:10289033
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	receptor; proteins; fv fragment; bacillus-subtilis; expression vector; scfv multimers; crystal-structure; monoclonal-antibody; escherichia-coli; effector-binding domain (en)
http://linked.open.../riv/klicoveSlovo	escherichia-coli expression vector crystal-structure bacillus-subtilis proteins receptor monoclonal-antibody effector-binding domain fv fragment scfv multimers
http://linked.open...odStatuVydavatele	DK - Dánské království
http://linked.open...ontrolniKodProRIV	[10DD91123DF9]
http://linked.open...i/riv/nazevZdroje	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	Biomolecular NMR spectroscopy for rational drug design
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	70
http://linked.open...iv/tvurceVysledku	Fábry, Milan Král, Vlastimil Řezáčová, Pavlína Veverka, Václav Sedláček, Juraj Škerlová, Jana
http://linked.open...ain/vavai/riv/wos	000345843300029
issn	1744-3091
number of pages	6 (xsd:int)
http://bibframe.org/vocab/doi	10.1107/S2053230X1402247X
http://localhost/t...ganizacniJednotka	11310

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