2HK6
Crystal Structure of B. subtilis ferrochelatase with Iron bound at the active site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-08 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.0605 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.650, 49.980, 118.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.640 - 1.710 |
| R-factor | 0.17824 |
| Rwork | 0.176 |
| R-free | 0.21951 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1doz |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.347 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.810 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.027 | |
| Number of reflections | 31884 | |
| Completeness [%] | 100.0 | 95.6 |
| Redundancy | 11.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8 | 288 | 25% PEG 2000, 0.2 M MgCl2, 0.1 M Tris-HCl , pH 8.0, VAPOR DIFFUSION, temperature 288K |
