5KNK
Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii with catalytic residue substitution (E127A)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2016-04-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.300, 145.470, 87.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 72.735 - 1.900 |
R-factor | 0.2265 |
Rwork | 0.225 |
R-free | 0.27120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kn7 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.100 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 72.740 |
High resolution limit [Å] | 1.900 |
Number of reflections | 30262 |
<I/σ(I)> | 7.95 |
Completeness [%] | 100.0 |
Redundancy | 1.9 |
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 200 mM KBr 2.2 M (NH4)2SO4 |