8BV9
Acylphosphatase from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-18 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 40.415, 81.944, 63.994 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.010 - 2.550 |
R-factor | 0.23894 |
Rwork | 0.233 |
R-free | 0.30077 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.639 |
Data reduction software | autoPROC |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.010 | 2.670 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.094 | 0.981 |
Rmeas | 0.109 | |
Rpim | 0.053 | |
Number of reflections | 3631 | 431 |
<I/σ(I)> | 10.2 | 1.5 |
Completeness [%] | 99.0 | |
Redundancy | 6.5 | |
CC(1/2) | 0.998 | 0.440 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.2 M AS 30% w/v PEG4K |