3RST
Crystal structure of Bacillus subtilis signal peptide peptidase A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-25 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 87.779, 131.066, 207.263 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.370 |
| R-factor | 0.20748 |
| Rwork | 0.206 |
| R-free | 0.24052 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bfo Chain A C-terminal Domain (residues 326-549) |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.135 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (for MR 2.1) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.370 | 2.370 |
| Rmerge | 0.085 | 0.294 |
| Number of reflections | 96535 | |
| <I/σ(I)> | 52.7 | 7.8 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 7.4 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291.15 | 100mM Tris pH 8.5 23% Tert-butanol 5% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K |
