3ZP9
Human Carbonic Anhydrase II as a Scaffold for an Artificial Transfer Hydrogenase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-12-13 |
Detector | DECTRIS PILATUS 2M |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.500, 41.620, 72.480 |
Unit cell angles | 90.00, 103.80, 90.00 |
Refinement procedure
Resolution | 40.011 - 1.310 |
R-factor | 0.1693 |
Rwork | 0.168 |
R-free | 0.19320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3pyk |
RMSD bond length | 0.018 |
RMSD bond angle | 1.790 |
Data reduction software | XDS |
Data scaling software | XSCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.010 | 1.380 |
High resolution limit [Å] | 1.310 | 1.310 |
Rmerge | 0.080 | 1.260 |
Number of reflections | 49267 | |
<I/σ(I)> | 9.3 | 1.26 |
Completeness [%] | 82.9 | 43.2 |
Redundancy | 3.2 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.9 | 293 | 2.1 M AMSO4, 50 MM TRIS-SO4, 0.2 MM 4-CHLOROMERCURIBENZOIC ACID, 4 MG/ML PROTEIN, PH 7.9, 293 K |