6WCD
Crystal Structure of Xenopus laevis APE2 Catalytic Domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 105 |
Detector technology | CCD |
Collection date | 2014-02-01 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.383, 73.149, 98.877 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.170 - 1.540 |
R-factor | 0.144 |
Rwork | 0.143 |
R-free | 0.15700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3g0r |
RMSD bond length | 0.014 |
RMSD bond angle | 1.346 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.170 | 1.600 |
High resolution limit [Å] | 1.540 | 1.540 |
Rmeas | 0.084 | 0.477 |
Number of reflections | 60632 | 5767 |
<I/σ(I)> | 16.14 | |
Completeness [%] | 99.3 | 94.99 |
Redundancy | 5.3 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 25% PEG 6000, 0.1 M MES pH 6.5, 2:1 and 1:1 protein:crystallant ratios |