1KXJ
The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-10-01 |
Detector | SBC-2 |
Wavelength(s) | 0.97916, 0.97938 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 82.045, 82.045, 176.352 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 * - 2.800 |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.27400 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.800 |
Data reduction software | HKL-2000 |
Data scaling software | d*TREK |
Phasing software | SnB |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.106 | 0.377 |
Number of reflections | 32696 | |
<I/σ(I)> | 12 | 2.2 |
Completeness [%] | 99.9 | 99.3 |
Redundancy | 3.7 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 21 * | 2 M mono-Ammonium dihydrogen Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | mono-ammonium dihydrogen phosphate | 2.0 (M) | |
2 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5 |