6UL2
Crystal structure of tryptophan-6-halogenase BorH complexed with L-tryptophan
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-08 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.480, 157.920, 113.250 |
| Unit cell angles | 90.00, 104.06, 90.00 |
Refinement procedure
| Resolution | 31.894 - 1.979 |
| R-factor | 0.1933 |
| Rwork | 0.193 |
| R-free | 0.22880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2oam |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.881 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.7.3) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 32.060 | 32.060 | 2.010 |
| High resolution limit [Å] | 1.979 | 10.840 | 1.980 |
| Rmerge | 0.162 | 0.114 | 0.798 |
| Rmeas | 0.182 | 0.129 | 0.895 |
| Rpim | 0.082 | 0.058 | 0.399 |
| Total number of observations | 4869 | 41453 | |
| Number of reflections | 170635 | 1030 | 8445 |
| <I/σ(I)> | 6 | 10.3 | 2.2 |
| Completeness [%] | 98.2 | 94.5 | 99.2 |
| Redundancy | 4.8 | 4.7 | 4.9 |
| CC(1/2) | 0.983 | 0.979 | 0.677 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.1 M Bis-Tris pH 6.5 300 mM (NH4)2SO4 19% (w/v) PEG 8000. |
