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 |