6EW5
Human myelin protein P2 F57A mutant, monoclinic crystal form
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 | 2012-06-14 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.125, 76.105, 138.425 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.490 - 1.950 |
R-factor | 0.1906 |
Rwork | 0.188 |
R-free | 0.23550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wut |
RMSD bond length | 0.005 |
RMSD bond angle | 0.932 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((dev_2006: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmeas | 0.173 | 0.821 |
Number of reflections | 40671 | 2958 |
<I/σ(I)> | 11.6 | 2.3 |
Completeness [%] | 99.1 | 98.7 |
Redundancy | 6 | 6 |
CC(1/2) | 0.994 | 0.754 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 40-42% PEG 6000 |