6AZS
Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-03-29 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.95373 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 62.067, 122.244, 136.061 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.900 - 1.590 |
R-factor | 0.15478 |
Rwork | 0.154 |
R-free | 0.17420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6azn |
RMSD bond length | 0.016 |
RMSD bond angle | 1.787 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.900 | 1.620 |
High resolution limit [Å] | 1.590 | 1.590 |
Rmerge | 0.183 | 1.122 |
Rpim | 0.074 | 0.530 |
Number of reflections | 139549 | 6791 |
<I/σ(I)> | 8.2 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 13.5 | 10.4 |
CC(1/2) | 0.996 | 0.665 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 281 | Sitting drops were set up with 150 nL protein at 7 mg/mL plus 300 nL reservoir: 100 mM bis-tris chloride buffer at pH 6.1, 23.6 (w/v) PEG 3350, 160 mM sodium thiocyanate |