1FOA
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F2 |
Synchrotron site | CHESS |
Beamline | F2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-01-23 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.541, 82.190, 101.956 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.250 - 1.800 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.22900 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.250 | 1.910 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.092 | 0.017 |
Total number of observations | 64537 * | |
Number of reflections | 42919 | |
<I/σ(I)> | 7.1 | |
Completeness [%] | 70.3 | 47.2 |
Redundancy | 1.5 | 1.64 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 * | 293 | PEG 8000, potassium chloride, glycerol, Tris, MES, UDP-GlcNAc, manganese chloride, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | MES | 10 (mM) | |
3 | 1 | drop | 270 (mM) | ||
4 | 1 | drop | 2 (mM) | ||
5 | 1 | drop | UDP-GlcNAc | 10 (mM) | |
6 | 1 | reservoir | PEG8000 | 15-25 (%) | |
7 | 1 | reservoir | Tris-HCl | 100 (mM) | |
8 | 1 | reservoir | glycerol | 0-5 (%) |