7OAC
conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form I
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 | 2020-06-15 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.9998 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 36.811, 37.365, 90.232 |
| Unit cell angles | 90.00, 98.98, 90.00 |
Refinement procedure
| Resolution | 34.459 - 2.150 |
| Rwork | 0.237 |
| R-free | 0.25760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7oaa |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.417 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049 2013/06/30) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.460 | 2.280 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.072 | 1.128 |
| Number of reflections | 13455 | 2156 |
| <I/σ(I)> | 13.37 | 1.61 |
| Completeness [%] | 99.7 | 99.9 |
| Redundancy | 6.61 | 6.78 |
| CC(1/2) | 1.000 | 0.700 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1M tri-sodium citrate pH 4.5, 7.1 % (w/v) PEG 10000 |
