3NTJ
Redox regulation of Plasmodium falciparum ornithine delta-aminotransferase
Experimental procedure
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Wavelength(s) | 0.979335 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 101.390, 104.970, 181.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.825 - 3.000 |
R-factor | 0.1944 |
Rwork | 0.191 |
R-free | 0.24230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1z7d |
RMSD bond length | 0.009 |
RMSD bond angle | 1.135 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.050 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.137 | 0.525 |
Number of reflections | 39278 | |
<I/σ(I)> | 14.4 | 3.6 |
Completeness [%] | 99.4 | 99.7 |
Redundancy | 3.6 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 2.2 M amonium sulfate, 100mM citriacidacid, 200m MKCL. Protein concentration in the drop 7.5 mg/ml., pH 8.0, VAPOR DIFFUSION, HANGING DROP |