2PFE
Crystal Structure of Thermobifida fusca Protease A (TFPA)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-05-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.95 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 130.959, 68.552, 40.355 |
| Unit cell angles | 90.00, 101.98, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.436 |
| R-factor | 0.2048 |
| Rwork | 0.202 |
| R-free | 0.22898 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2.1A structure of TFPA |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.329 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.460 |
| High resolution limit [Å] | 1.436 | 1.436 |
| Rmerge | 0.076 | 0.352 |
| Number of reflections | 61453 | |
| <I/σ(I)> | 15.52 | 2.6 |
| Completeness [%] | 96.9 | 87.8 |
| Redundancy | 4 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 8% (v/v) glycerol, 10mM MnCl2, 0.15M AmSO4, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
