3PDX
Crystal structural of mouse tyrosine aminotransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Wavelength(s) | 1.0809 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 69.275, 84.839, 157.992 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.940 - 2.910 |
R-factor | 0.26516 |
Rwork | 0.263 |
R-free | 0.29522 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dyd |
RMSD bond length | 0.017 |
RMSD bond angle | 1.718 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.086 | 0.388 |
Number of reflections | 10641 | |
<I/σ(I)> | 24.4 | 2.3 |
Redundancy | 6 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | 20% PEG 4000, 100 mM cacodylic acid buffer, and 20% glycerol. , pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |