6STS
Human myelin protein P2 mutant R30Q
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 | 2011-04-19 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.590, 75.960, 100.630 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
Rwork | 0.254 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wut |
RMSD bond length | 0.003 |
RMSD bond angle | 0.592 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.080 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmeas | 0.142 | 1.885 |
Number of reflections | 9332 | 665 |
<I/σ(I)> | 9 | 1.2 |
Completeness [%] | 98.4 | 95.5 |
Redundancy | 4.7 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 3.6 M ammonium sulphate, 10% glycerol |