2ICX
Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UTP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-05-02 |
Detector | BRUKER PROTEUM-R |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 187.683, 59.679, 89.813 |
Unit cell angles | 90.00, 100.38, 90.00 |
Refinement procedure
Resolution | 70.481 - 1.850 |
R-factor | 0.195 |
Rwork | 0.192 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1z90 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.902 |
Data reduction software | SAINT |
Data scaling software | SAINT |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 70.481 | 70.481 | 1.900 |
High resolution limit [Å] | 1.850 | 5.050 | 1.850 |
Rmerge | 0.035 | 0.014 | 0.311 |
Number of reflections | 83235 | ||
<I/σ(I)> | 23.9 | 72.84 | 3.19 |
Completeness [%] | 99.4 | 98.1 | 100 |
Redundancy | 14.3 | 5.09 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | vapor diffusion, hanging drop with micro-seeding | 273 | Protein solution (10 mg/ml protein, 0.050 M sodium chloride, 0.0003 M TCEP, 0.005 M Tris PH 8.0) mixed in a 1:1 ratio with Well solution ( 28 % PEG 2K, 5% DMSO, 0.10 M MES/Acetate pH 5.5), crystals soaked in well solution supplemented with 0.002 M UTP, vapor diffusion, hanging drop with micro-seeding, temperature 273K |