1NSL
Crystal structure of Probable acetyltransferase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | SBC-2 |
Wavelength(s) | 0.984 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.339, 134.185, 91.062 |
Unit cell angles | 90.00, 104.08, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.700 |
R-factor | 0.25808 |
Rwork | 0.256 |
R-free | 0.28550 * |
Structure solution method | MAD |
RMSD bond length | 0.021 * |
RMSD bond angle | 2.337 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.450 |
Rmerge | 0.102 * |
Number of reflections | 48725 * |
Completeness [%] | 100.0 * |
Redundancy | 2.40 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 10 (%) | |
3 | 1 | reservoir | sodium potassium phosphate | pH6.0 | |
4 | 1 | reservoir | 0.1 (M) |