6IL2
K4U complex structure of peptide deformylase from Xanthomonas oryzae pv. oryzae
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 | 2018-03-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97940 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 58.531, 58.531, 266.212 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.900 - 2.410 |
R-factor | 0.1939 |
Rwork | 0.192 |
R-free | 0.23190 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5e5d |
RMSD bond length | 0.018 |
RMSD bond angle | 2.072 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
Rmerge | 0.184 | 0.120 | 0.485 |
Rmeas | 0.189 | 0.123 | 0.509 |
Rpim | 0.042 | 0.026 | 0.148 |
Number of reflections | 11239 | 678 | 539 |
<I/σ(I)> | 12 | ||
Completeness [%] | 98.3 | 95.5 | 98.2 |
Redundancy | 15.8 | 20.6 | 10.5 |
CC(1/2) | 0.996 | 0.546 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7.5 | 287 | 0.05M cadmium sulfate, 0.1M HEPES pH 7.5, 2.0M sodium acetate trihydrate |