4GXW
Crystal structure of a cog1816 amidohydrolase (target EFI-505188) from Burkhoderia ambifaria, with bound Zn
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-13 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.058, 66.223, 75.432 |
| Unit cell angles | 90.00, 93.64, 90.00 |
Refinement procedure
| Resolution | 29.257 - 1.300 |
| R-factor | 0.1612 |
| Rwork | 0.160 |
| R-free | 0.18140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pao |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.081 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 75.280 | 75.280 | 1.370 |
| High resolution limit [Å] | 1.300 | 4.110 | 1.300 |
| Rmerge | 0.073 | 0.029 | 0.567 |
| Total number of observations | 20082 | 72987 | |
| Number of reflections | 175186 | ||
| <I/σ(I)> | 10.9 | 18.3 | 1.3 |
| Completeness [%] | 99.5 | 97.6 | 98.3 |
| Redundancy | 3.5 | 3.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | sitting drop vapor diffusion | 6.5 | 298 | Protein (20 mM Hepes pH 7.5; Reservoir (0.2 M magnesium chloride, 0.1 M MES pH 6.5, 10% Peg4000); Cryoprotection (Reservoir, + 20% Diethylene glycol), sitting drop vapor diffusion, temperature 298K |
