6A0E
Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 5C (4A) |
Synchrotron site | PAL/PLS |
Beamline | 5C (4A) |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9796 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 83.153, 84.903, 87.198 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.415 - 1.947 |
R-factor | 0.1766 |
Rwork | 0.174 |
R-free | 0.22350 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.489 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Rpim | 0.037 | 0.276 |
Number of reflections | 45885 | 2264 |
<I/σ(I)> | 21.18 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.3 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 295 | PEG 3350, Potassium phosphate monobasic |