4JBD
Crystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrate
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 | 2013-02-14 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 44.529, 54.166, 142.656 |
| Unit cell angles | 90.00, 96.57, 90.00 |
Refinement procedure
| Resolution | 22.118 - 1.300 |
| R-factor | 0.1593 |
| Rwork | 0.158 |
| R-free | 0.18400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2azp |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.283 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (0.1.27) |
| Phasing software | AMoRE |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.859 | 1.320 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.062 | 0.735 |
| Number of reflections | 82749 | |
| <I/σ(I)> | 7.9 | 1.4 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 298 | Protein (15 mM Hepes pH 8.0, 150 mM NaCl, 5% glycerol, 10 mM PYRROLE-2-CARBOXYLATE); Reservoir (0.2 M di-Ammonium Hydrogen Citrate, 20 %(w/v) PEG 3350). Soak 2 minutes in (Reservoir + 20% Glycerol), VAPOR DIFFUSION, SITTING DROP, temperature 298K |
