4DRP
Evaluation of Synthetic FK506 Analogs as Ligands for the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-3-(3,4-dimethoxyphenyl)-1-((S)-1-(2-((1R,2S)-2-ethyl-1-hydroxy-cyclohexyl)-2-oxoacetyl)piperidine-2-carbonyloxy)propyl)phenoxy)acetic acid from cocrystallization
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-03-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.900 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.913, 56.563, 57.589 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.2221 |
Rwork | 0.220 |
R-free | 0.26090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3o5q |
RMSD bond length | 0.013 |
RMSD bond angle | 1.472 |
Data scaling software | SCALA (3.2.25) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 25.386 | 25.386 | 1.890 |
High resolution limit [Å] | 1.792 | 5.670 | 1.790 |
Rmerge | 0.062 | 0.034 | 0.190 |
Total number of observations | 1752 | 4333 | |
Number of reflections | 15448 | ||
<I/σ(I)> | 12.4 | 15.8 | 3.9 |
Completeness [%] | 97.5 | 97.2 | 84 |
Redundancy | 3.3 | 3.1 | 2.3 |
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 |