5CHO
Crystal Structure of BorF, the Flavin Reductase Component of a Bacterial Two-Component Tryptophan Halogenase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.988 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 278.010, 62.340, 101.880 |
| Unit cell angles | 90.00, 110.84, 90.00 |
Refinement procedure
| Resolution | 47.607 - 2.370 |
| R-factor | 0.2158 |
| Rwork | 0.215 |
| R-free | 0.24680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hx6 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.990 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.937 | 2.490 |
| High resolution limit [Å] | 2.370 | 2.370 |
| Rmerge | 0.100 | 0.820 |
| Number of reflections | 64289 | |
| <I/σ(I)> | 9.4 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.6 | 295.15 | Drop containing 1 uL of 10 mg/mL (0.474 mM) BorF in 20 mM Tris pH 7.5, 100 mM NaCl, with 1 mM FAD mixed with 1 uL of reservoir solution containing 20% PEG 400, 0.1 M HEPES pH 7.6, 5% v/v glycerol against 200 micro liter reservoir |
