6XVQ
Human myelin protein P2 mutant K31Q
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 | 2011-03-24 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.91 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 58.240, 58.240, 102.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.800 |
R-factor | 0.1477 |
Rwork | 0.145 |
R-free | 0.19220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wut |
RMSD bond length | 0.009 |
RMSD bond angle | 1.001 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.850 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmeas | 0.117 | 0.981 |
Number of reflections | 16817 | 1217 |
<I/σ(I)> | 19 | 2.5 |
Completeness [%] | 98.7 | 99.8 |
Redundancy | 9.5 | 9.2 |
CC(1/2) | 0.999 | 0.780 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 277 | 32% PEG 6000, 0.1 M citrate pH 5.0 |