1HRK
CRYSTAL STRUCTURE OF HUMAN FERROCHELATASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-10-20 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 93.433, 87.569, 109.699 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.870 - 2.000 |
| R-factor | 0.202 |
| Rwork | 0.202 |
| R-free | 0.22600 |
| Structure solution method | SAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | CrystalClear |
| Data scaling software | SCALEPACK (V. 1.9.1) |
| Phasing software | ISAS |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.990 |
| High resolution limit [Å] | 2.000 | 1.950 |
| Rmerge | 0.058 | 0.117 |
| Number of reflections | 60384 | |
| <I/σ(I)> | 48 | 12 |
| Completeness [%] | 98.4 | 98.2 |
| Redundancy | 20 | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | Burden, A.E., (1999) Biochim.Biophys.Acta, 1435, 191. * |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | Burden, A.E., (1999) Biochim.Biophys.Acta, 1435, 191. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | HEPES | 0.1 (M) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | PEG400 | 32 (%) | |
| 4 | 1 | reservoir | sodium phosphate | 0.1 (M) |
