6XVS
Human myelin protein P2 mutant P38G, unliganded
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-05 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 1.03 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.540, 65.490, 82.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.1703 |
Rwork | 0.167 |
R-free | 0.22480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wut |
RMSD bond length | 0.012 |
RMSD bond angle | 1.167 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_2247) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmeas | 0.054 | 0.664 |
Number of reflections | 25915 | 1211 |
<I/σ(I)> | 21.8 | 2.2 |
Completeness [%] | 91.0 | 58.4 |
Redundancy | 5.5 | |
CC(1/2) | 0.999 | 0.770 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 277 | 40% PEG 1000, 0.1 M citrate pH 5.0 |