1DHY
KKS102 BPHC ENZYME
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-06-11 |
| Detector | MARRESEARCH |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 123.000, 123.000, 110.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.800 * |
| R-factor | 0.204 * |
| Rwork | 0.186 |
| R-free | 0.24300 * |
| RMSD bond length | 0.011 * |
| RMSD bond angle | 1.910 * |
| Data reduction software | WEIS |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.800 * |
| Rmerge | 0.076 * |
| Total number of observations | 200071 * |
| Number of reflections | 34668 * |
| Completeness [%] | 88.4 * |
| Redundancy | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 12 * | Sugiyama, K., (1995) Proteins: Struct. Funct. Genet., 22, 284. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 17 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.9 (M) | |
| 3 | 1 | reservoir | MPD | 10 (%) | |
| 4 | 1 | reservoir | Tris-HCl | 100 (mM) | pH7.5 |






