5WBH
Structure of the FRB domain of mTOR bound to a substrate recruitment peptide of S6K1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97920 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 60.613, 80.944, 134.848 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.010 - 1.750 |
| R-factor | 0.1937 |
| Rwork | 0.193 |
| R-free | 0.21020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fap |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.066 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.068 | 0.040 | 0.603 |
| Rmeas | 0.076 | 0.045 | 0.680 |
| Rpim | 0.032 | 0.019 | 0.304 |
| Total number of observations | 328879 | ||
| Number of reflections | 66487 | 6153 | |
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 98.2 | 97.3 | 92.4 |
| Redundancy | 4.9 | 5 | 4 |
| CC(1/2) | 0.998 | 0.727 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 289 | tacsimate |
