1KN9
CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD MECHANISM.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-12-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.08000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 112.441, 112.441, 198.675 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 * - 2.400 |
| R-factor | 0.239 |
| Rwork | 0.239 |
| R-free | 0.27800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b12 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.452 * |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.041 | 0.296 |
| Total number of observations | 277201 * | |
| Number of reflections | 49984 | |
| <I/σ(I)> | 25.4 | 5.8 |
| Completeness [%] | 98.8 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 * | 22 * | ammonium dihydrogen phosphate, sodium citrate, Triton X-100, pH 5.4, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.4 |
| 3 | 1 | drop | Triton X-100 | 0.5 (%) | |
| 4 | 1 | reservoir | ammonium dihydrogen phosphate | 0.70 (M) | |
| 5 | 1 | reservoir | sodium citrate | 0.1 (M) | pH5.4 |
