6H6X
Structure of an evolved dimeric form of the UbiD-class enzyme HmfF from Pelotomaculum thermopropionicum in complex with prFMN
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 | 2016-02-24 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 167.720, 63.930, 98.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 83.860 - 2.250 |
| R-factor | 0.19667 |
| Rwork | 0.194 |
| R-free | 0.24772 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6h6v |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.910 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 83.860 | 2.130 |
| High resolution limit [Å] | 2.080 | 2.080 |
| Rmeas | 0.070 | 0.920 |
| Number of reflections | 279066 | |
| <I/σ(I)> | 12.1 | 1.7 |
| Completeness [%] | 97.3 | 98.1 |
| Redundancy | 4.5 | 4.5 |
| CC(1/2) | 1.000 | 0.600 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 294 | 0.12 M alcohols, 0.1 M NaHEPES/MOPS buffer pH 7.5, 20% v/v ethylene glycol and 10% w/v PEG 8000 |
