Optimization of the crystallizability of a single-chain antibody fragment
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10289033" target="_blank" >RIV/00216208:11310/14:10289033 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/14:00438427 RIV/61388963:_____/14:00438427
Result on the web
<a href="http://dx.doi.org/10.1107/S2053230X1402247X" target="_blank" >http://dx.doi.org/10.1107/S2053230X1402247X</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S2053230X1402247X" target="_blank" >10.1107/S2053230X1402247X</a>
Alternative languages
Result language
angličtina
Original language name
Optimization of the crystallizability of a single-chain antibody fragment
Original language 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-engineeringapproaches 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-fragmentstability and homogeneity. Such an optimization of the protein storage buffer led to a significantly improved ability of the scFv MEM-57 to yield crystals.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/LK11205" target="_blank" >LK11205: Biomolecular NMR spectroscopy for rational drug design</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091
e-ISSN
—
Volume of the periodical
70
Issue of the periodical within the volume
December 2014
Country of publishing house
DK - DENMARK
Number of pages
6
Pages from-to
1701-1706
UT code for WoS article
000345843300029
EID of the result in the Scopus database
—