7ABB
The truncated structure of the Bottromycin biosynthetic protein SalCYP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-08-25 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.9801 |
Spacegroup name | P 41 |
Unit cell lengths | 96.538, 96.538, 49.999 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.269 - 1.500 |
R-factor | 0.164302924969 |
Rwork | 0.163 |
R-free | 0.18117 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7aba |
RMSD bond length | 0.008 |
RMSD bond angle | 0.966 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | AutoSol |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 68.260 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.072 | 0.889 |
Number of reflections | 73906 | 10737 |
<I/σ(I)> | 15.1 | |
Completeness [%] | 100.0 | |
Redundancy | 9.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | PEG8000, Glycerol, Magnesium acetate, Sodium cacodylate |