5WBL
Crystal structure of the Arabidopsis thaliana Raptor in complex with the TOS peptide of human PRAS40
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, 151.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.350 |
R-factor | 0.2074 |
Rwork | 0.205 |
R-free | 0.26562 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5wbi |
RMSD bond length | 0.008 |
RMSD bond angle | 1.344 |
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 | 3.470 |
High resolution limit [Å] | 3.350 | 7.220 | 3.350 |
Rmerge | 0.088 | 0.033 | 0.758 |
Rmeas | 0.098 | 0.037 | 0.850 |
Rpim | 0.042 | 0.015 | 0.377 |
Total number of observations | 115461 | ||
Number of reflections | 22827 | 2209 | |
<I/σ(I)> | 10 | ||
Completeness [%] | 98.5 | 98.7 | 97.6 |
Redundancy | 5.1 | 5.4 | 4.8 |
CC(1/2) | 0.999 | 0.770 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 289 | tacsimate |