2H1W
Crystal structure of the His183Ala mutant variant of Bacillus subtilis ferrochelatase
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 | 2005-11-27 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.940, 49.720, 116.540 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.300 - 2.600 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.25900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1doz |
RMSD bond length | 0.008 |
RMSD bond angle | 1.200 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.300 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 16593 | |
Completeness [%] | 95.8 | 91.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.4 | 288 | 25-30 % PEG2000, 0.2 M magnesium chloride, 0.1 M Tris-HCl, pH 7.4, VAPOR DIFFUSION, temperature 288K |