2CAH
STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH
Replaces: 1CAFExperimental procedure
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Detector technology | FILM |
| Collection date | 1994 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 112.360, 112.360, 249.140 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 2.700 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PMC WITH NADPH AT 3.1 A RESOLUTION |
| RMSD bond length | 0.015 |
| RMSD bond angle | 3.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 2.823 | 2.820 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.049 | |
| Number of reflections | 24337 | |
| Completeness [%] | 92.0 | 92.4 |
| Redundancy | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 4-5 * | Jouve, H.M., (1991) J.Mol.Biol., 221, 1075. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 27 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 100 (mM) | |
| 3 | 1 | drop | glycerol | 2.5 (%(v/v)) | |
| 4 | 1 | drop | ammonium sulfate | 1 (M) | |
| 5 | 1 | drop | 25 (mM) | ||
| 6 | 1 | reservoir | ammonium sulfate | 2 (M) | |
| 7 | 1 | reservoir | 50 (mM) | ||
| 8 | 1 | reservoir | Tris-HCl | 100 (mM) |
