3T90
Crystal structure of glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-27 |
Detector | RAYONIX MX-225 |
Wavelength(s) | 0.933 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 68.520, 47.174, 42.223 |
Unit cell angles | 90.00, 100.74, 90.00 |
Refinement procedure
Resolution | 26.880 - 1.500 |
R-factor | 0.16659 |
Rwork | 0.165 |
R-free | 0.20111 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vez |
RMSD bond length | 0.026 |
RMSD bond angle | 2.211 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.900 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 21167 | |
<I/σ(I)> | 44.8 | 14.8 |
Completeness [%] | 99.7 | 100 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 30% PEG 1000, 0.1M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |