3QU1
Peptide deformylase from Vibrio cholerae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9195 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 74.296, 74.296, 127.219 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.200 - 1.800 |
| R-factor | 0.1688 |
| Rwork | 0.167 |
| R-free | 0.20370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bs6 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.625 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 33.200 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.104 | 0.065 | 0.879 |
| Number of reflections | 33867 | ||
| <I/σ(I)> | 8.2 | 2.43 | |
| Completeness [%] | 100.0 | 99.5 | 100 |
| Redundancy | 13.4 | 12.3 | 10.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 0.2 M magnesium chloride, 0.1 M Tris-HCl buffer, 25% PEG-3350, 10 mM zinc sulfate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
