7OAH
conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta2/A
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 | 2017-07-10 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 26.126, 38.769, 132.277 |
Unit cell angles | 90.00, 94.85, 90.00 |
Refinement procedure
Resolution | 37.190 - 1.694 |
Rwork | 0.220 |
R-free | 0.26780 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7oaa |
RMSD bond length | 0.007 |
RMSD bond angle | 1.008 |
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] | 37.190 | 1.800 |
High resolution limit [Å] | 1.690 | 1.690 |
Rmerge | 0.082 | 0.912 |
Number of reflections | 29121 | 4428 |
<I/σ(I)> | 13.73 | 1.78 |
Completeness [%] | 97.9 | 92.6 |
Redundancy | 6.66 | 6.76 |
CC(1/2) | 1.000 | 0.860 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1 M tri-sodium citrate pH 5.5, 20% (w/v) PEG 3000 |