1FB5
LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-02-10 |
Detector | MARRESEARCH |
Spacegroup name | P 43 3 2 |
Unit cell lengths | 184.700, 184.700, 184.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 3.500 |
R-factor | 0.219 |
Rwork | 0.212 |
R-free | 0.25000 * |
RMSD bond length | 0.010 |
RMSD bond angle | 23.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 500.000 | 3.920 |
High resolution limit [Å] | 3.500 | 3.510 |
Rmerge | 0.160 | 0.320 |
Number of reflections | 13959 | |
<I/σ(I)> | 4.3 | |
Completeness [%] | 98.2 | 99.5 |
Redundancy | 10 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 298 | 8% PEG 4000, 0.1 M Na acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7-9 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 10 (mM) | pH7.4 |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | |
4 | 1 | reservoir | PEG4000 | 8 (%(w/v)) | pH4.6 |