7OAF
conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form III
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 | 26.010, 38.849, 128.811 |
Unit cell angles | 90.00, 96.18, 90.00 |
Refinement procedure
Resolution | 33.214 - 1.450 |
Rwork | 0.198 |
R-free | 0.21500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7oaa |
RMSD bond length | 0.018 |
RMSD bond angle | 1.654 |
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] | 33.214 | 1.540 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.083 | 0.835 |
Number of reflections | 45592 | 7257 |
<I/σ(I)> | 11.32 | 1.77 |
Completeness [%] | 99.8 | 99.4 |
Redundancy | 6.62 | 6.3 |
CC(1/2) | 1.000 | 0.960 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1M tri-sodium citrate pH 4.5, 9.3% PEG 6000 |