6XUW
Human myelin protein P2 mutant L27D
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 | 2010-11-19 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.97 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 64.880, 64.880, 100.920 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.310 |
R-factor | 0.1908 |
Rwork | 0.188 |
R-free | 0.24530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wut |
RMSD bond length | 0.003 |
RMSD bond angle | 0.530 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.10_2140) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.370 |
High resolution limit [Å] | 2.310 | 2.310 |
Rmeas | 0.232 | 2.208 |
Number of reflections | 9951 | 653 |
<I/σ(I)> | 8 | 0.9 |
Completeness [%] | 98.9 | 94.6 |
Redundancy | 7.9 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 291 | 38% PEG 6000, 0.1 M citrate, pH 5.0 |