2ES4
Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 183.000, 75.700, 116.600 |
| Unit cell angles | 90.00, 117.60, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.850 |
| Rwork | 0.199 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cvl |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.072 | 0.521 |
| Number of reflections | 120503 | |
| <I/σ(I)> | 15.4 | 3.85 |
| Completeness [%] | 99.0 | 91.3 |
| Redundancy | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 20 % PEG3350, 0.2 M KI, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
