6JEW
K3U bound crystal peptide deformylase from Acinetobacter baumanii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 5C (4A) |
Synchrotron site | PAL/PLS |
Beamline | 5C (4A) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-10-18 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97950 |
Spacegroup name | P 32 |
Unit cell lengths | 39.493, 39.493, 187.119 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.990 - 2.000 |
R-factor | 0.229 |
Rwork | 0.226 |
R-free | 0.29240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6jer |
RMSD bond length | 0.015 |
RMSD bond angle | 1.872 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
High resolution limit [Å] | 2.000 | 5.430 | 2.000 |
Rmerge | 0.127 | 0.102 | 0.370 |
Rmeas | 0.146 | 0.117 | 0.444 |
Rpim | 0.071 | 0.056 | 0.242 |
Number of reflections | 21486 | 945 | 1062 |
<I/σ(I)> | 14 | ||
Completeness [%] | 97.2 | 83.8 | 97.3 |
Redundancy | 3.8 | 4.3 | 3 |
CC(1/2) | 0.972 | 0.711 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8.5 | 287 | 0.03 M MgCl2, 0.03 M CaCl2, 15% (v/v) PEGMME, 15% (w/v) PEG 20000, 0.1 M Tris (base)/ Bicine pH 8.5 |