3BK9
H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX10.1 |
| Synchrotron site | SRS |
| Beamline | PX10.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-01-30 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.381 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.222, 117.606, 139.283 |
| Unit cell angles | 90.00, 95.73, 90.00 |
Refinement procedure
| Resolution | 54.130 - 2.150 |
| R-factor | 0.2047 |
| Rwork | 0.200 |
| R-free | 0.28457 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nw7 |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.346 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.660 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.100 | 0.474 |
| Number of reflections | 131764 | |
| <I/σ(I)> | 9.5 | 2.5 |
| Completeness [%] | 96.9 | 91.7 |
| Redundancy | 2.4 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 293 | 100mM Mes (pH 6.3), 10-12% (wt/vol) PEG 4000, 60mM MnCl2, 10mM sodium dithionite, 2mM L-Trp, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
