3FIX
Crystal structure of a putative n-acetyltransferase (ta0374) from thermoplasma acidophilum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-08-11 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 |
Unit cell lengths | 42.229, 60.915, 72.116 |
Unit cell angles | 101.19, 90.10, 89.97 |
Refinement procedure
Resolution | 30.000 - 2.300 |
R-factor | 0.23215 |
Rwork | 0.230 |
R-free | 0.27555 |
Structure solution method | SAD |
RMSD bond length | 0.022 |
RMSD bond angle | 1.999 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.5.0051) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.051 | 0.380 |
Number of reflections | 30257 | |
Completeness [%] | 97.1 | 91.2 |
Redundancy | 2 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | 0.1 M HEPES, 10% (w/v) PEG 8000, 10% (w/v) ETHYLENE GLYCOL , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |