1OZN
1.5A Crystal Structure of the Nogo Receptor Ligand Binding Domain Reveals a Convergent Recognition Scaffold Mediating Inhibition of Myelination
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-12-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0064, 1.0096, 0.9950 |
Spacegroup name | P 1 |
Unit cell lengths | 32.206, 33.915, 60.221 |
Unit cell angles | 85.02, 75.91, 67.96 |
Refinement procedure
Resolution | 50.000 - 1.520 |
R-factor | 0.168 |
Rwork | 0.167 |
R-free | 0.19800 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 26.500 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.560 |
High resolution limit [Å] | 1.520 | 1.520 |
Rmerge | 0.053 | 0.214 |
Number of reflections | 33484 | |
<I/σ(I)> | 34 | 7.4 |
Completeness [%] | 96.6 | 96.4 |
Redundancy | 14.4 | 13.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 * | 298 | PEG4000, sodium chloride, sodium acetate, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 35 (%) | |
3 | 1 | reservoir | 0.25 (M) | ||
4 | 1 | reservoir | sodium acetate | 0.1 (M) | pH6.5 |