3FWX
The crystal structure of the peptide deformylase from Vibrio cholerae O1 biovar El Tor str. N16961
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 | 2008-12-05 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9794 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 61.305, 61.456, 210.343 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 105.410 - 2.000 |
R-factor | 0.20506 |
Rwork | 0.202 |
R-free | 0.26234 |
Structure solution method | SAD |
RMSD bond length | 0.024 |
RMSD bond angle | 1.922 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 105.410 | 2.052 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.097 | 0.661 |
Number of reflections | 25897 | |
<I/σ(I)> | 14.72 | 1.9 |
Completeness [%] | 99.5 | 100 |
Redundancy | 9.5 | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 10mM Sodium citrate, 33% PEG 6000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |