4DRI
Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of mTOR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-09-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9788 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.503, 59.554, 67.787 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.050 - 1.450 |
| R-factor | 0.1784 |
| Rwork | 0.177 |
| R-free | 0.20640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fap |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.546 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.1) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 67.787 | 67.787 | 1.530 |
| High resolution limit [Å] | 1.450 | 4.590 | 1.450 |
| Rmerge | 0.043 | 0.030 | 0.377 |
| Total number of observations | 7198 | 20445 | |
| Number of reflections | 41315 | ||
| <I/σ(I)> | 17.3 | 18.2 | 2 |
| Completeness [%] | 95.7 | 97.7 | 93.8 |
| Redundancy | 3.8 | 4.9 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | 25% PEG3350, 0.1 M NaCl, 0.1M HEPES-NaOH pH 7.5, vapor diffusion, temperature 293K |
