5HWE
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 | 2014-03-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.95370 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 70.341, 82.563, 114.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.500 - 1.710 |
| R-factor | 0.15289 |
| Rwork | 0.151 |
| R-free | 0.19447 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bvq |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.912 |
| 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] | 41.500 | 1.740 |
| High resolution limit [Å] | 1.707 | 1.707 |
| Number of reflections | 36498 | |
| <I/σ(I)> | 13.2 | 2.3 |
| Completeness [%] | 99.7 | 93.8 |
| Redundancy | 7.2 | 6.4 |
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; reservoir of 2.45 M ammonium sulfate, 10% glycerol |
