5WBK
Crystal structure of the arabidopsis thaliana Raptor in complex with the TOS peptide of human 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 21 21 21 |
| Unit cell lengths | 89.100, 113.100, 152.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.110 |
| R-factor | 0.21101 |
| Rwork | 0.209 |
| R-free | 0.25463 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5wbi |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.314 |
| 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] | 80.000 | 80.000 | 3.210 |
| High resolution limit [Å] | 3.100 | 6.680 | 3.100 |
| Rmerge | 0.084 | 0.027 | 0.819 |
| Rmeas | 0.091 | 0.030 | 0.885 |
| Rpim | 0.035 | 0.013 | 0.331 |
| Total number of observations | 182755 | ||
| Number of reflections | 27998 | 2759 | |
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 99.2 | 98.1 | 99.4 |
| Redundancy | 6.5 | 5.5 | 6.9 |
| CC(1/2) | 0.999 | 0.846 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 289 | tacsimate |
