7OP4
Crystal structure of the computationally designed SAKe6BE-3HH protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-05-06 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.00003 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 44.049, 76.290, 67.987 |
| Unit cell angles | 90.00, 90.02, 90.00 |
Refinement procedure
| Resolution | 38.150 - 1.520 |
| R-factor | 0.1853 |
| Rwork | 0.184 |
| R-free | 0.20210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Design model |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.19.2-4158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.150 | 38.150 | 1.550 |
| High resolution limit [Å] | 1.520 | 8.330 | 1.520 |
| Rmerge | 0.037 | 0.033 | 0.206 |
| Rmeas | 0.040 | 0.035 | 0.222 |
| Rpim | 0.015 | 0.013 | 0.082 |
| Total number of observations | 234771 | 1501 | 11746 |
| Number of reflections | 33235 | 220 | 1624 |
| <I/σ(I)> | 28.8 | 56.6 | 8.4 |
| Completeness [%] | 96.3 | 98.8 | 96.3 |
| Redundancy | 7.1 | 6.8 | 7.2 |
| CC(1/2) | 1.000 | 0.999 | 0.990 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293.15 | 0.1 M MES, 0.9 M Na phosphate, 0.9 M K phosphate |
