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. |