2PO5
Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-06-25 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 93.420, 87.730, 109.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.900 - 2.200 |
R-factor | 0.209 |
Rwork | 0.209 |
R-free | 0.24000 |
Structure solution method | DIFFERENCE FOURIER |
RMSD bond length | 0.005 |
RMSD bond angle | 1.211 |
Data reduction software | DENZO (1.9.1) |
Data scaling software | SCALEPACK (1.9.1) |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.065 |
Number of reflections | 45450 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 2 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (50 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA- CHOLATE, 250 MM IMIDAZOLE, PH 8.1) AND PRECIPITANT SOLUTION (0.1 M HEPES PH 7.5, 0.2 M AMMONIUM SULFATE, 34% PEG 400, 0.1 M SODIUM PHOSPHATE)., pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 291K |