3E0X
The crystal structure of a Lipase-esterase related protein from Clostridium acetobutylicum ATCC 824
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 | 2008-04-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.611, 75.153, 68.206 |
| Unit cell angles | 90.00, 97.89, 90.00 |
Refinement procedure
| Resolution | 38.100 - 1.450 |
| R-factor | 0.14525 |
| Rwork | 0.143 |
| R-free | 0.18455 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.387 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.100 | 1.480 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.092 | 0.490 |
| Number of reflections | 75965 | |
| <I/σ(I)> | 28.9 | 2.28 |
| Completeness [%] | 96.3 | 75.8 |
| Redundancy | 4.2 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.2M LiCl 20% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
