4JFI
Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with compound 1-[(9S,13R,13aR)-1,3-dimethoxy-8-oxo-5,8,9,10,11,12,13,13a-octahydro-6H-9,13-epiminoazocino[2,1-a]isoquinolin-14-yl]-2-(3,4,5-trimethoxyphenyl)ethane-1,2-dione
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-16 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.051, 54.192, 55.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.050 |
R-factor | 0.1382 |
Rwork | 0.137 |
R-free | 0.15800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.025 |
RMSD bond angle | 2.190 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.2.25) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 27.984 | 27.984 | 1.110 |
High resolution limit [Å] | 1.050 | 3.320 | 1.050 |
Rmerge | 0.061 | 0.036 | 0.402 |
Total number of observations | 10077 | 24107 | |
Number of reflections | 57507 | ||
<I/σ(I)> | 16.2 | 15.9 | 1.7 |
Completeness [%] | 95.3 | 94.2 | 72.9 |
Redundancy | 5.5 | 5.1 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 293 | 37.5% PEG3350, 0.1 M NH4OAc, 0.1 M HEPES pH 7.5, 10% DMSO, vapor diffusion, temperature 293K |