4NV4
1.8 Angstrom Crystal Structure of Signal Peptidase I from Bacillus anthracis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-26 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 80.225, 80.225, 174.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.810 - 1.800 |
| R-factor | 0.17403 |
| Rwork | 0.173 |
| R-free | 0.19940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4me8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.558 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0046) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.056 | 0.512 |
| Number of reflections | 31574 | |
| <I/σ(I)> | 30 | 3.9 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7.1 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 295 | Protein: 7.3 mG/mL, 0.25 M Sodium chloride, 0.01 M Tris-HCL buffer pH 8.3; Screen: Classics II (H11), 0.1M Potassium thiocyanate, 30% (w/v) PEG 2000 MME., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
