3OCA
Crystal structure of peptide deformylase from Ehrlichia chaffeensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-21 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9744 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 84.260, 64.430, 80.910 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.670 - 2.400 |
R-factor | 0.195 |
Rwork | 0.192 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1n5n |
RMSD bond length | 0.013 |
RMSD bond angle | 1.283 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.460 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.069 | 0.487 |
Number of reflections | 17678 | |
<I/σ(I)> | 18.6 | 3.4 |
Completeness [%] | 99.2 | 99.8 |
Redundancy | 4.8 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | 200MM AMMONIUM CITRATE, 20% PEG 3350; Protein at 28MG/ML, PH 8.5, VAPOR DIFFUSION, VAPOR DIFFUSION, SITTING DROP, temperature 290K |