1JB3
The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 0.95, 0.97842, 0.97928, 1.2 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 76.130, 49.460, 53.280 |
Unit cell angles | 90.00, 116.40, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.600 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.24300 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SHARP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.060 * | 0.325 * |
Number of reflections | 22609 | |
<I/σ(I)> | 5 | 5 |
Completeness [%] | 94.3 | 93.6 * |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 * | 4 * | PEG4000, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | reservoir | citrate | 0.1 (M) | |
3 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
4 | 1 | reservoir | 2-propanol | 20 (%(w/v)) | |
5 | 1 | reservoir | MPD | 20 (%(w/v)) |