1GP3
Human IGF2R domain 11
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-09-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 31.373, 49.843, 83.030 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.350 - 1.950 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gp0 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.330 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.090 | 0.653 |
| Total number of observations | 75027 * | |
| Number of reflections | 9752 | |
| <I/σ(I)> | 21.9 | 2.4 |
| Completeness [%] | 97.2 | 92.9 |
| Redundancy | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 3 * | PROTEIN WAS CRYSTALLIZED FROM 0.2 M SODIUM ACETATE, 0.1 M TRIS HCL PH 8.5, 30 % W/V PEG 4000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 100 (mM) | pH3.0 |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | reservoir | sodium acetate | 0.2 (M) | |
| 5 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
| 6 | 1 | reservoir | PEG4000 | 30 (%) |
