4Z04
Crystal structure of a probable lactoylglutathione lyase from Brucella melitensis in complex with glutathione
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-12 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.97872 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 82.630, 39.500, 41.700 |
| Unit cell angles | 90.00, 116.29, 90.00 |
Refinement procedure
| Resolution | 20.622 - 1.450 |
| R-factor | 0.1351 |
| Rwork | 0.134 |
| R-free | 0.16110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4qb5 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.020 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.490 |
| High resolution limit [Å] | 1.450 | 6.480 | 1.450 |
| Rmerge | 0.034 | 0.027 | 0.308 |
| Rmeas | 0.040 | 0.032 | 0.383 |
| Total number of observations | 84185 | ||
| Number of reflections | 21264 | 212 | 1427 |
| <I/σ(I)> | 20.5 | 39.01 | 2.97 |
| Completeness [%] | 98.4 | 78.8 | 89.1 |
| Redundancy | 3.96 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | Molecular Dimensions, Morpheus e4: 30mM each: Di-Ethyleneglycol, Tri-Ethyleneglycol, TetraEthyleneglycol, Penta-Ethyleneglycol; 100mM Imidazole/MES pH 6.5; 12.5% each MPD (racemic), PEG 1K, PEG 3350; BrabA.17481.b.B1.PS02324 at 21.7mg/ml with 8mM Gluathione; Cryo: direct; tray 261781e4; puck epp4-1 |
