6XIX
Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 |
| Unit cell lengths | 72.950, 76.550, 93.590 |
| Unit cell angles | 118.40, 89.61, 103.06 |
Refinement procedure
| Resolution | 70.570 - 2.100 |
| Rwork | 0.178 |
| R-free | 0.22830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6azo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.561 |
| Data reduction software | XDS (BUILT=20180319) |
| Data scaling software | XDS (BUILT=20180319) |
| Phasing software | MOLREP (11.0) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 81.570 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.068 | 0.176 |
| Number of reflections | 91216 | 12132 |
| <I/σ(I)> | 9.16 | 4.76 |
| Completeness [%] | 90.4 | 92.2 |
| Redundancy | 2.13 | 2.16 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 1 uL 20 mg/mL protein + 1 uL 24% PEG6000, 0.1 M Bis-Tris propane |
