3RRI
Crystal structure of glyoxalase/bleomycin resistance protein/dioxygenase from Alicyclobacillus acidocaldarius
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97932 |
| Spacegroup name | I 4 |
| Unit cell lengths | 104.728, 104.728, 49.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.500 |
| R-factor | 0.13563 |
| Rwork | 0.135 |
| R-free | 0.15911 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | different crystal form of the same protein that was solved by SAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.470 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.093 | 0.827 |
| Number of reflections | 43267 | |
| <I/σ(I)> | 32 | 2.5 |
| Completeness [%] | 99.6 | 99.6 |
| Redundancy | 10 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1 M Bis/Tris propane:NaOH, 2.8 M sodium acetate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
