Experimental procedure
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 283 |
| Detector technology | IMAGE PLATE |
| Collection date | 1990-07-07 |
| Detector | RIGAKU RAXIS IV++ |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 157.200, 157.200, 201.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 7.000 - 1.600 |
| R-factor | 0.211 |
| Rwork | 0.211 |
| Structure solution method | MIR STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.100 * |
| Data reduction software | WEIS |
| Data scaling software | SCALE |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.670 |
| High resolution limit [Å] | 1.500 | 1.600 |
| Rmerge | 0.069 | |
| Total number of observations | 1131480 * | |
| Number of reflections | 277449 | |
| Completeness [%] | 49 | |
| Redundancy | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | Andersson, I., (1983) J. Biol. Chem., 258, 14088. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | ||
| 2 | 1 | drop | 0.05 (M) | ||
| 3 | 1 | drop | PEG6000 | 8-15 (%) | |
| 4 | 1 | reservoir | 0.05 (M) | ||
| 5 | 1 | reservoir | PEG6000 | 8-15 (%) | |
| 6 | 1 | reservoir | 0.1 (M) |
