6DKT
Crystal structure of Arginase from Bacillus subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-09-12 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 77.140, 128.550, 82.020 |
Unit cell angles | 90.00, 112.69, 90.00 |
Refinement procedure
Resolution | 47.701 - 2.080 |
R-factor | 0.2048 |
Rwork | 0.204 |
R-free | 0.23090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4g3h |
RMSD bond length | 0.005 |
RMSD bond angle | 0.733 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.701 | 2.150 |
High resolution limit [Å] | 2.080 | 2.080 |
Rmerge | 0.060 | 0.280 |
Rmeas | 0.085 | 0.396 |
Number of reflections | 88598 | 8819 |
<I/σ(I)> | 6.26 | 1.92 |
Completeness [%] | 100.0 | 100 |
Redundancy | 1.9 | 1.8 |
CC(1/2) | 0.993 | 0.803 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 100 mM Bis Tris, 14.5% PEG3350, 5% PGA |