1N0I
Crystal Structure of Ferrochelatase with Cadmium bound at active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | AREA DETECTOR |
| Collection date | 2000-09-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.02916 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.415, 49.878, 118.777 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.000 * - 2.000 |
| R-factor | 0.231 |
| Rwork | 0.231 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1doz |
| RMSD bond length | 0.006 |
| RMSD bond angle | 21.500 * |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 * | 2.200 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.241 * | 0.289 * |
| Number of reflections | 19585 | |
| Completeness [%] | 97.3 | 97.1 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 * | 298 | Hansson, M., (1995) Proteins: Struct.,Funct., Genet., 23, 607. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 0.65 (mg/ml) | |
| 2 | 1 | drop | PEG2000 | 2.5 (%) | |
| 3 | 1 | drop | 17 (mM) | ||
| 4 | 1 | drop | Tris-HCl | 8 (mM) | |
| 5 | 1 | reservoir | PEG2000 | 30 (%(w/v)) | |
| 6 | 1 | reservoir | 0.2 (M) | ||
| 7 | 1 | reservoir | Tris-HCl | 0.1 (M) |
