1PV8
Crystal structure of a low activity F12L mutant of human porphobilinogen synthase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-10-08 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 63 |
Unit cell lengths | 89.571, 89.571, 153.190 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.000 - 2.200 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.28600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e51 |
RMSD bond length | 0.018 |
RMSD bond angle | 23.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.050 | 0.200 |
Number of reflections | 33615 * | |
Completeness [%] | 95.7 | 72.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 296 | 50mM BTP, 10mM beta-mercaptoethanol, 10uM ZnCl2, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4.0 (mg/ml) | |
2 | 1 | reservoir | monoammonium hydrogen phosphate | 0.4 (M) |