6XJM
Biuret Hydrolase (BiuH) from Rhodococcus sp. Mel C169S bound with biuret
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-03-15 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.991840 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.290, 103.340, 133.870 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.060 - 2.050 |
| Rwork | 0.184 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6azo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.640 |
| Data reduction software | XDS (BUILT=20200131) |
| Data scaling software | XSCALE (BUILT=20200131) |
| Phasing software | MOLREP (11.0) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 81.800 | 2.150 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.124 | 0.425 |
| Number of reflections | 102760 | 13718 |
| <I/σ(I)> | 8.42 | 3.66 |
| Completeness [%] | 99.7 | 99.9 |
| Redundancy | 4.25 | 4.32 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 1uL 5 mg/mL protein + 1uL 20% w/v PEG3350, 0.2M MgCl2, 20mM Biuret pH 5.5 |
