7OAA
conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-08-29 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 1.0704 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 38.243, 38.243, 279.665 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.890 - 1.400 |
| Rwork | 0.231 |
| R-free | 0.26850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5apt |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.687 |
| Data reduction software | XDS |
| Data scaling software | STARANISO |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049 2013/06/30) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.890 | 1.470 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.054 | 0.662 |
| Number of reflections | 10751 | 538 |
| <I/σ(I)> | 24.3 | 3.7 |
| Completeness [%] | 91.5 | |
| Redundancy | 17.6 | |
| CC(1/2) | 1.000 | 0.978 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1M HEPES pH 7.5, 30% (w/v) PEG 300 |






