5UG4
Structure of spermidine N-acetyltransferase SpeG from Vibrio cholerae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-17 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97857 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 71.884, 134.635, 137.346 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.150 |
R-factor | 0.17088 |
Rwork | 0.169 |
R-free | 0.19986 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mi4 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.919 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.200 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.090 | 0.390 |
Number of reflections | 36218 | |
<I/σ(I)> | 28.5 | 8.3 |
Completeness [%] | 99.4 | 98.2 |
Redundancy | 14.9 | 15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.1 M Tris, 50% MPD, 20% ethanol |