5WIF
Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Yersinia pestis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-04-11 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 102.596, 120.114, 122.752 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.19087 |
Rwork | 0.188 |
R-free | 0.24189 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5cnp |
RMSD bond length | 0.019 |
RMSD bond angle | 1.955 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.050 | 0.660 |
Number of reflections | 26195 | 1292 |
<I/σ(I)> | 30.6 | 2.7 |
Completeness [%] | 99.7 | 100 |
Redundancy | 5.7 | 5.9 |
CC(1/2) | 0.900 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1 M MIB buffer, 25% (w/v) PEG 1500 |