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 |
