2G3A
Crystal structure of putative acetyltransferase from Agrobacterium tumefaciens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-02-10 |
Detector | SBC |
Wavelength(s) | 0.97924 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 60.768, 94.675, 57.145 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.900 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.22700 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.144 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.920 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.093 | 0.390 |
Number of reflections | 13028 | |
<I/σ(I)> | 32.7 | 3.7 |
Completeness [%] | 97.4 | 82 |
Redundancy | 7.8 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M Hepes, pH 8.0, 0.1M CaCl2, 28% PEG 400, 3% MPD, 1mM AcetylCOA, VAPOR DIFFUSION, SITTING DROP, temperature 293K |