2OLG
Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 4A |
| Synchrotron site | PAL/PLS |
| Beamline | 4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-01-15 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.229, 53.304, 116.643 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.420 - 1.700 |
| R-factor | 0.2078 |
| Rwork | 0.204 |
| R-free | 0.24454 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2any |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.452 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.067 | 0.258 |
| Number of reflections | 26625 | |
| <I/σ(I)> | 34 | 3 |
| Completeness [%] | 98.4 | 96 |
| Redundancy | 7.7 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 287 | 0.15M lithium sulfate, 30% polyethylene glycol 4000, 0.1M Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K |
