| PAVELČÍK, František a Jiří VÁCLAVÍK. Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. HOBOKEN: WILEY-BLACKWELL, 2010, roč. 66, s. 1012-1023. ISSN 0907-4449. Dostupné z: https://dx.doi.org/10.1107/S0907444910030234. |
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@article{1757816,
author = {Pavelčík, František and Václavík, Jiří},
article_location = {HOBOKEN},
doi = {http://dx.doi.org/10.1107/S0907444910030234},
keywords = {rotation function; translation function; conformation function; automatic model building; generalized atoms; flexible-group model; tripeptides; tetrapeptides; real-space refinement},
language = {eng},
issn = {0907-4449},
journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
title = {Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments},
volume = {66},
year = {2010}
}
TY - JOUR
ID - 1757816
AU - Pavelčík, František - Václavík, Jiří
PY - 2010
TI - Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments
JF - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
VL - 66
SP - 1012-1023
EP - 1012-1023
PB - WILEY-BLACKWELL
SN - 09074449
KW - rotation function
KW - translation function
KW - conformation function
KW - automatic model building
KW - generalized atoms
KW - flexible-group model
KW - tripeptides
KW - tetrapeptides
KW - real-space refinement
N2 - The automatic building of protein structures with tripeptidic and tetrapeptidic fragments was investigated. The oligopeptidic conformers were positioned in the electron-density map by a phased rotation, conformation and translation function and refined by a real-space refinement. The number of successfully located fragments lay within the interval 75-95% depending on the resolution and phase quality. The overlaps of partially located fragments were analyzed. The correctly positioned fragments were connected into chains. Chains formed in this way were extended directly into the electron density and a sequence was assigned. In the initial stage of the model building the number of located fragments was between 60% and 95%, but this number could be increased by several cycles of reciprocal-space refinement and automatic model rebuilding. A nearly complete structure can be obtained on the condition that the resolution is reasonable. Computer graphics will only be needed for a final check and small corrections.
ER -
PAVELČÍK, František a Jiří VÁCLAVÍK. Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments. \textit{ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}. HOBOKEN: WILEY-BLACKWELL, 2010, roč.~66, s.~1012-1023. ISSN~0907-4449. Dostupné z: https://dx.doi.org/10.1107/S0907444910030234.
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