3S8L
Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing Hydrophobic Surface Area
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2011-05-22 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 42.072, 42.072, 108.755 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.240 - 1.710 |
| R-factor | 0.19887 |
| Rwork | 0.196 |
| R-free | 0.25558 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ov1 |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.990 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.770 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Number of reflections | 9628 | |
| <I/σ(I)> | 12.8 | 3.8 |
| Completeness [%] | 85.1 | |
| Redundancy | 2.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1 M HEPES, 3.5 M sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
