8AQ3
In surfo structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli in complex with PE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-04 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.96861 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 160.994, 160.994, 91.282 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.376 - 2.395 |
R-factor | 0.2255 |
Rwork | 0.225 |
R-free | 0.23960 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5n6l |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_3494) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.480 | 2.540 |
High resolution limit [Å] | 2.395 | 2.400 |
Rmeas | 0.140 | 2.920 |
Number of reflections | 53802 | 8590 |
<I/σ(I)> | 12.46 | 0.88 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 11.1 | 11.22 |
CC(1/2) | 0.990 | 0.460 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 291 | 50 mM sodium acetate pH 5.0, 50 mM magnesium acetate and 28-36 %(v/v) PEG200 |