3OAI
Crystal structure of the extra-cellular domain of human myelin protein zero
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 173 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-06-21 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.9779 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.900, 54.886, 146.069 |
| Unit cell angles | 90.00, 98.54, 90.00 |
Refinement procedure
| Resolution | 19.960 - 2.100 |
| R-factor | 0.18643 |
| Rwork | 0.183 |
| R-free | 0.25227 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.472 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
| Rmerge | 0.087 | ||
| Number of reflections | 77053 | ||
| Completeness [%] | 99.9 | 100 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 11.1 | 297 | 40% PEG 8000, 0.1 M KSCN, 0.1 M Tris, pH 11.1, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
