2BPI
Structure of Iron dependent superoxide dismutase from P. falciparum.
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 | 2003-07-06 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.941, 78.910, 90.621 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 59.760 - 2.520 |
| R-factor | 0.187 |
| Rwork | 0.183 |
| R-free | 0.26300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1isc |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.453 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.590 |
| High resolution limit [Å] | 2.520 | 2.500 |
| Rmerge | 0.080 | 0.300 |
| Number of reflections | 13247 | |
| <I/σ(I)> | 17.3 | 6.2 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4.1 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1M TRIS PH 7.5,38% PEG 600 |
