5HY1
high resolution structure of barbiturase
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 | CCD |
Collection date | 2014-03-30 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.95370 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 69.403, 82.356, 114.552 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.200 - 2.010 |
R-factor | 0.1876 |
Rwork | 0.186 |
R-free | 0.22273 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5hwe |
RMSD bond length | 0.010 |
RMSD bond angle | 1.196 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.200 | 2.060 |
High resolution limit [Å] | 2.010 | 2.010 |
Number of reflections | 22146 | |
<I/σ(I)> | 24.6 | 3.5 |
Completeness [%] | 99.6 | 95.2 |
Redundancy | 14.4 | 13.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Protein at 16 mg/,mL in 50 mM ADA pH 6.5, 50 mM NaCl mixed with 2.45 M ammonium sulfate, 10% glycerol; 150 nL plus 150 nL |