1DUV
CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 86.680, 134.230, 109.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.700 |
R-factor | 0.194 |
Rwork | 0.192 |
R-free | 0.22100 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.046 | 0.235 |
Number of reflections | 119653 | |
<I/σ(I)> | 18.7 | |
Completeness [%] | 85.8 | 34.7 |
Redundancy | 2.7 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | PEG 8000, PEG 1000, HEPES, DTT , pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 17.8 (%(w/v)) | |
3 | 1 | reservoir | PEG1000 | 2.2 (%(w/v)) |