6H6V
Structure of the UbiD-class enzyme HmfF from Pelotomaculum thermopropionicum in complex with FMN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-02-17 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.910, 139.250, 136.880 |
| Unit cell angles | 90.00, 93.74, 90.00 |
Refinement procedure
| Resolution | 74.200 - 2.660 |
| R-factor | 0.20097 |
| Rwork | 0.199 |
| R-free | 0.23599 |
| Structure solution method | MAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.580 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.200 | 2.730 |
| High resolution limit [Å] | 2.660 | 2.660 |
| Rmeas | 0.144 | 1.103 |
| Number of reflections | 343818 | 6736 |
| <I/σ(I)> | 9.8 | 1.6 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 3.8 | 3.8 |
| CC(1/2) | 1.000 | 0.500 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.1 M Tris/BICINE buffer pH 8.5, 20% v/v ethylene glycol and 10% w/v PEG 8000 |
