1WS0
Structure analysis of peptide deformylase from Bacillus cereus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 6B |
| Synchrotron site | PAL/PLS |
| Beamline | 6B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-05-10 |
| Detector | BRUKER PROTEUM 300 |
| Wavelength(s) | 1.12714 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.330, 42.802, 84.806 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.920 - 1.700 |
| R-factor | 0.215 |
| Rwork | 0.200 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Number of reflections | 24095 | |
| Completeness [%] | 90.7 | 27.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.5 | 295 | MES, PEG6000, pH 5.5, VAPOR DIFFUSION, temperature 295K |
