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 |