1R0C
Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-12 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.928 |
Spacegroup name | H 3 |
Unit cell lengths | 128.776, 128.776, 198.017 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.370 |
R-factor | 0.228 |
Rwork | 0.226 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1d09 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.424 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.450 |
High resolution limit [Å] | 2.370 | 2.370 |
Number of reflections | 46167 | |
<I/σ(I)> | 12 | 2.1 |
Completeness [%] | 92.8 | 75.5 |
Redundancy | 2 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | PEG 4000, Hepes-Na, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |