1Q1Y
Crystal Structures of Peptide Deformylase from Staphylococcus aureus Complexed with Actinonin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-06-21 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.072 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 94.417, 120.844, 48.057 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 1.900 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 22.900 * |
| Data reduction software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 1.900 |
| Number of reflections | 21798 |
| <I/σ(I)> | 29.2 |
| Completeness [%] | 98.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 297 * | PEG4000, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 30 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 25 (mM) | pH7.5 |
| 3 | 1 | drop | 200 (mM) | ||
| 4 | 1 | reservoir | PEG4000 | 23 (%(w/v)) | |
| 5 | 1 | reservoir | Tris-HCl | 50 (mM) | pH8.5 |
| 6 | 1 | reservoir | glycerol | 15 (%(v/v)) | |
| 7 | 1 | reservoir | 100 (mM) | ||
| 8 | 1 | reservoir | 20 (mM) |
