2ZAT
Crystal structure of a mammalian reductase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 42 |
Unit cell lengths | 109.612, 109.612, 94.308 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.500 |
R-factor | 0.162 |
Rwork | 0.161 |
R-free | 0.18700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cyd |
RMSD bond length | 0.014 |
RMSD bond angle | 1.540 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 176173 | |
<I/σ(I)> | 5.3 | 2.4 |
Completeness [%] | 99.1 | 98.1 |
Redundancy | 6.4 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1.2M sodium acetate, 20%(v/v) glycerol, 0.1M Hepes/NaOH buffer, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K |