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 |
