1UA8
Crystal structure of the lipoprotein localization factor, LolA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-11-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.998 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.590, 60.590, 79.030 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| Rwork | 0.226 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1iwl |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.039 * | 0.256 * |
| Number of reflections | 13592 | |
| Completeness [%] | 99.4 | 99.5 |
| Redundancy | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.4 * | 20 * | PEG1500, Tris-HCl, Glycerol, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | pH7.4 |
| 3 | 1 | reservoir | PEG1500 | 15 (%(w/v)) | |
| 4 | 1 | reservoir | Tris-HCl | 20 (mM) | pH8.0 |
| 5 | 1 | reservoir | glycerol | 20 (%(v/v)) |
