1E2T
Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Wavelength(s) | 0.933, 0.979 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 134.530, 222.419, 104.662 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.800 |
| R-factor | 0.264 |
| Rwork | 0.264 |
| R-free | 0.30200 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.810 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (0.5) |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.800 |
| Rmerge | 0.059 * |
| Total number of observations | 235995 * |
| Number of reflections | 73897 |
| <I/σ(I)> | 8.3 |
| Completeness [%] | 94.7 |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.9 * | 20 * | pH 6.80 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | dithiothreitol | 3 (mM) | |
| 5 | 1 | reservoir | Na/K tartrate | 0.8 (M) | |
| 6 | 1 | reservoir | MES | 0.1 (M) |
