1OLZ
The ligand-binding face of the semaphorins revealed by the high resolution crystal structure of SEMA4D
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-06-20 |
Detector | ADSC CCD |
Spacegroup name | P 1 |
Unit cell lengths | 73.320, 76.760, 89.410 |
Unit cell angles | 77.41, 73.35, 63.57 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.27000 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 28.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.099 | 0.801 |
Total number of observations | 375205 * | |
Number of reflections | 108424 | |
<I/σ(I)> | 17.6 | 1.8 |
Completeness [%] | 97.2 | 90.9 |
Redundancy | 3.5 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 * | 0.2 M AMMONIUM FLORIDE, 20% PEG 3350, pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 0.1 (M) | pH8.0 |
3 | 1 | drop | 0.1 (M) |