4D6B
Human myelin protein P2, mutant P38G
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 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 64.311, 64.311, 101.362 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.335 - 2.116 |
| R-factor | 0.2211 |
| Rwork | 0.218 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wut |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.667 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.170 |
| High resolution limit [Å] | 2.120 | 2.120 |
| Rmerge | 0.050 | 0.760 |
| Number of reflections | 12434 | |
| <I/σ(I)> | 23.5 | 1.7 |
| Completeness [%] | 97.8 | 84.9 |
| Redundancy | 7.7 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |






