1QD6
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID2 |
| Synchrotron site | ESRF |
| Beamline | ID2 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-09-13 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 80.067, 84.038, 95.245 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.300 - 2.100 |
| R-factor | 0.226 |
| Rwork | 0.226 |
| R-free | 0.28300 |
| Starting model (for MR) | MONOMER OMPLA (1QD5) WITHOUT WATER/DETERGENT MOLECULES |
| RMSD bond length | 0.007 |
| RMSD bond angle | 27.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.300 | 2.170 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.077 | 0.265 |
| Number of reflections | 28336 | |
| <I/σ(I)> | 10.9 | |
| Completeness [%] | 74.1 | 66.7 |
| Redundancy | 2.69 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6.5 * | 293 | protein solution is mixed in a 3:2 ratio with well solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | succinate | 10 (mM) | |
| 3 | 1 | drop | beta-OG | 1.5 (%) | |
| 4 | 1 | drop | 1 (mM) | ||
| 5 | 1 | reservoir | 1 (mM) | ||
| 6 | 1 | reservoir | bis-Tris | 0.1 (M) |
