TY - JOUR
T1 - The PDZ2 domain of syntenin at ultra-high resolution
T2 - Bridging the gap between macromolecular and small molecule crystallography
AU - Kang, Beom Sik
AU - Devedjiev, Yancho
AU - Derewenda, Urszula
AU - Derewenda, Zygmunt S.
PY - 2004/4/30
Y1 - 2004/4/30
N2 - The crystal structure of the second PDZ domain of the scaffolding protein syntenin was solved using data extending to 0.73Å resolution. The crystallographic model, including the hydrogen atoms and the anisotropic displacement parameters, was refined to a conventional R-factor of 7.5% and Rfree of 8.7%, making it the most precise crystallographic model of a protein molecule to date. The model reveals discrete disorder in several places in the molecule, and significant plasticity of the peptide bond, with some ω angles deviating by nearly 20°from planarity. Most hydrogen atoms are easily identifiable in the electron density and weak hydrogen bonds of the C-H⋯O type are clearly visible between the β-strands. The study sets a new standard for high-resolution protein crystallography.
AB - The crystal structure of the second PDZ domain of the scaffolding protein syntenin was solved using data extending to 0.73Å resolution. The crystallographic model, including the hydrogen atoms and the anisotropic displacement parameters, was refined to a conventional R-factor of 7.5% and Rfree of 8.7%, making it the most precise crystallographic model of a protein molecule to date. The model reveals discrete disorder in several places in the molecule, and significant plasticity of the peptide bond, with some ω angles deviating by nearly 20°from planarity. Most hydrogen atoms are easily identifiable in the electron density and weak hydrogen bonds of the C-H⋯O type are clearly visible between the β-strands. The study sets a new standard for high-resolution protein crystallography.
KW - Crystallography
KW - LHB, lost hydrogen bond
KW - PDZ
KW - PEG, polyethylene glycol
KW - Syntenin
KW - Ultra-high resolution
UR - http://www.scopus.com/inward/record.url?scp=1842635588&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2004.02.057
DO - 10.1016/j.jmb.2004.02.057
M3 - Article
C2 - 15081807
AN - SCOPUS:1842635588
SN - 0022-2836
VL - 338
SP - 483
EP - 493
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -