2OS1
Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes
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 | 2004-11-26 |
Detector | BRUKER PROTEUM 300 |
Wavelength(s) | 1.12714 |
Spacegroup name | P 43 |
Unit cell lengths | 67.999, 67.999, 41.127 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.040 - 1.500 |
R-factor | 0.186 |
Rwork | 0.186 |
R-free | 0.19800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lqy |
RMSD bond length | 0.014 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.450 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.052 | 0.283 |
Number of reflections | 37104 | |
<I/σ(I)> | 28.3 | 4.5 |
Completeness [%] | 86.4 | 19.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 294 | 16% PEG 8000, 0.2M Ammonium sulfate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294K |