4HTG
Porphobilinogen Deaminase from Arabidopsis Thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 141.573, 37.271, 55.069 |
| Unit cell angles | 90.00, 105.00, 90.00 |
Refinement procedure
| Resolution | 32.890 - 1.450 |
| R-factor | 0.14859 |
| Rwork | 0.145 |
| R-free | 0.21707 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pda |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.052 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.890 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.098 | 0.767 |
| Number of reflections | 49235 | |
| <I/σ(I)> | 5.6 | 2.2 |
| Completeness [%] | 99.3 | 99.4 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 5 mg/ml protein added in 50:50 ratio to the well-solution of 25% PEG 4000, 100 mM sodium citrate, 200 mM ammonium sulphate. Crystals grown in the dark due to photosensitivity of the cofactor., pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
