2W79
Establishing wild-type levels of catalytic activity on natural and artificial (ba)8-barrel protein scaffolds
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.000, 64.100, 79.200 |
| Unit cell angles | 90.00, 94.00, 90.00 |
Refinement procedure
| Resolution | 33.630 - 1.850 |
| R-factor | 0.206 |
| Rwork | 0.202 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qo2 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.319 |
| Data reduction software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.960 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.050 | 0.540 |
| Number of reflections | 42406 | |
| <I/σ(I)> | 13.4 | 2.5 |
| Completeness [%] | 98.9 | 97.5 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1 M TRIS-HCL PH 7.5, 25% PEG 3350 |
