6NKH
Structure of MalC Reductase/Diels-Alderase from Malbranchea aurantiaca
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-02-08 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.033 |
Spacegroup name | P 42 |
Unit cell lengths | 79.368, 79.368, 133.586 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.970 - 1.600 |
R-factor | 0.1699 |
Rwork | 0.166 |
R-free | 0.19880 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.864 |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.970 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 107859 | |
<I/σ(I)> | 15.4 | 1.4 |
Completeness [%] | 99.2 | 92.1 |
Redundancy | 6.6 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 293 | 32% PEG 2K MME, 0.1 M sodium acetate, 0.1 M MES pH 6.5 |