6MVF
Crystal structure of FMN-binding beta-glucuronidase from Facaelibacterium prausnitzii L2-6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-08-10 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 129.556, 106.815, 183.823 |
| Unit cell angles | 90.00, 90.29, 90.00 |
Refinement procedure
| Resolution | 29.524 - 2.550 |
| R-factor | 0.168 |
| Rwork | 0.167 |
| R-free | 0.22610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3cmg |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.981 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.520 | 2.641 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.121 | 0.570 |
| Number of reflections | 163078 | 16164 |
| <I/σ(I)> | 11.22 | 2.58 |
| Completeness [%] | 99.6 | 99.53 |
| Redundancy | 5 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 11.1 mg/mL protein, 0.2 M magnesium chloride, 10% w/v PEG 3000, 0.1 M sodium cacodylate |
