6S6N
Crystal structure of the Gorilla LL37(17-29) antimicrobial peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-05-12 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.873 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 41.150, 41.150, 57.280 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.640 - 1.100 |
R-factor | 0.1613 |
Rwork | 0.160 |
R-free | 0.17880 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Poly Ala alpha-helix |
RMSD bond length | 0.014 |
RMSD bond angle | 1.708 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 35.640 | 35.640 | 1.130 |
High resolution limit [Å] | 1.100 | 4.910 | 1.100 |
Rmerge | 0.056 | 0.042 | 0.552 |
Rmeas | 0.057 | 0.044 | 0.598 |
Total number of observations | 222293 | ||
Number of reflections | 12186 | 184 | 808 |
<I/σ(I)> | 31.12 | 63.46 | 3.14 |
Completeness [%] | 99.4 | 100 | 92.1 |
Redundancy | 18.242 | 16.598 | 6.433 |
CC(1/2) | 0.999 | 0.998 | 0.904 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | Reservoir contained 0.1 M HEPES pH 7.5, 1.4 M sodium citrate |