4R6F
Crystal structure of computational designed protein DLRR_I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-15 |
| Detector | RIGAKU SATURN 70 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.135, 42.571, 67.607 |
| Unit cell angles | 90.00, 102.14, 90.00 |
Refinement procedure
| Resolution | 66.100 - 1.730 |
| R-factor | 0.15875 |
| Rwork | 0.156 |
| R-free | 0.20388 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Computational designed template |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.922 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (MR) |
| Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 66.100 | 1.950 | 1.790 |
| High resolution limit [Å] | 1.730 | 1.860 | 1.730 |
| Number of reflections | 31150 | ||
| <I/σ(I)> | 33.7 | 12.7 | 4.7 |
| Completeness [%] | 96.3 | 90.6 | 84.1 |
| Redundancy | 10.3 | 3 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 24% PEG 3350, 0.1 M HEPES, 0.2 M Ammonium Sulfate, 0.1 M Proline, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
