2FZK
The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.50 Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 2005-03-31 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 120.900, 120.900, 141.610 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.450 - 2.500 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.23890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1za2 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.450 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.075 | 0.370 |
Number of reflections | 41523 | |
<I/σ(I)> | 13 | 3.9 |
Completeness [%] | 99.1 | 99.6 |
Redundancy | 4.96 | 4.78 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 5.7 | 298 | ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7), MICRODIALYSIS, temperature 298K |