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 |