4LC0
Identifying ligand binding hot spots in proteins using brominated fragments
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 146.830, 98.440, 39.700 |
| Unit cell angles | 90.00, 95.79, 90.00 |
Refinement procedure
| Resolution | 30.805 - 2.221 |
| R-factor | 0.1627 |
| Rwork | 0.161 |
| R-free | 0.20050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h9g |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.159 |
| Data scaling software | Aimless (0.1.29) |
| Phasing software | PHASER (2.5.4) |
| Refinement software | PHENIX (dev_1370) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.810 | 30.810 | 2.280 |
| High resolution limit [Å] | 2.220 | 9.930 | 2.220 |
| Rmerge | 0.081 | 0.054 | 0.237 |
| Total number of observations | 1024 | 6115 | |
| Number of reflections | 27508 | ||
| <I/σ(I)> | 14.3 | 28.1 | 5.8 |
| Completeness [%] | 90.3 | 86.4 | 74.2 |
| Redundancy | 1.7 | 1.6 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 292 | 1.8M ammonium sulfate, 15% sucrose, 0.1M Tris-HCl, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
