4LBW
Identifying ligand binding hot spots in proteins using brominated fragments
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.900 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 147.220, 98.490, 39.700 |
| Unit cell angles | 90.00, 95.68, 90.00 |
Refinement procedure
| Resolution | 30.810 - 1.741 |
| R-factor | 0.1717 |
| Rwork | 0.171 |
| R-free | 0.19430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h9g |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.145 |
| Data scaling software | Aimless (0.1.29) |
| Phasing software | PHASER (2.5.4) |
| Refinement software | PHENIX (dev_1370) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.810 | 1.790 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Rmerge | 0.053 | 0.698 |
| Total number of observations | 16042 | |
| Number of reflections | 57511 | |
| <I/σ(I)> | 17.6 | 2 |
| Completeness [%] | 97.9 | 98.7 |
| Redundancy | 1.8 | 1.8 |
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 |
