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 | 112.409, 112.409, 136.550 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.213 |
| R-free | 0.25700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.300 | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.089 * | 0.420 * |
| Total number of observations | 275832 * | |
| Number of reflections | 38611 | |
| <I/σ(I)> | 14 | 2.1 |
| Completeness [%] | 97.7 | 99.6 |
| Redundancy | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.8 | 4 * | Raves, M.L., (1997) Nature Struct.Biol., 4, 57. * |
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) |
