5BK6
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 | 62.130, 122.678, 135.745 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.800 - 1.590 |
R-factor | 0.15124 |
Rwork | 0.150 |
R-free | 0.17420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6azn |
RMSD bond length | 0.018 |
RMSD bond angle | 1.893 |
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] | 45.800 | 1.620 |
High resolution limit [Å] | 1.590 | 1.590 |
Rmerge | 0.071 | 0.726 |
Rpim | 0.045 | 0.588 |
Number of reflections | 139814 | 6816 |
<I/σ(I)> | 11.7 | 1.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.1 | 4.3 |
CC(1/2) | 0.999 | 0.627 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | Sitting drops were set up with 150 nL protein at 100 mg/mL plus 150 nL reservoir: 100 mM bis-tris chloride buffer at pH 5.5, 17% (w/v) PEG 10000, 100 mM sodium acetate |