Experimental procedure
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 273 |
| Detector technology | IMAGE PLATE |
| Collection date | 1993-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 112.410, 112.410, 136.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ACE |
| RMSD bond length | 0.014 * |
| RMSD bond angle | 1.980 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.095 * | 0.621 * |
| Total number of observations | 138332 * | |
| Number of reflections | 46243 | |
| <I/σ(I)> | 7.4 | 0.9 |
| Completeness [%] | 96.6 | 96.7 |
| Redundancy | 1.9 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.8 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 35% PEG 200, 100 MM MES, PH 5.8, AT 4 DEG., temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG200 | 38 (%) | |
| 2 | 1 | reservoir | MES | 0.1 (M) | |
| 3 | 1 | drop | protein | 12 (mg/ml) |
