Experimental procedure
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X31 |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Collection date | 1993-11 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 |
| Unit cell lengths | 77.300, 77.300, 77.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 1.670 |
| R-factor | 0.153 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cdv |
| RMSD bond length | 0.030 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((ROTAVATA)) |
| Phasing software | SHELXL-93 |
| Refinement software | SHELXL-93 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.300 | 1.710 |
| High resolution limit [Å] | 1.670 | 1.670 |
| Rmerge | 0.079 | 0.265 |
| Number of reflections | 28861 | |
| <I/σ(I)> | 8.1 | 2.8 |
| Completeness [%] | 94.3 | 89.6 |
| Redundancy | 8.1 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | PROTEIN WAS CRYSTALLIZED FROM 75% (V/V) ETHANOL AND 0.05 M SODIUM ACETATE (PH 5.5) |
