9CP9
Crystal structure of DHPS-3-dehydrogenase, HpsN H319A variant from Cupriavidus pinatubonensis in complex with substrate (R-DHPS) and NADH
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2024-07-05 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.95372 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.324, 75.809, 84.674 |
Unit cell angles | 90.00, 117.10, 90.00 |
Refinement procedure
Resolution | 42.299 - 2.013 |
Rwork | 0.167 |
R-free | 0.19360 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 1.245 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.820 | 2.060 |
High resolution limit [Å] | 2.010 | 2.010 |
Number of reflections | 62003 | 4296 |
<I/σ(I)> | 7.6 | 1.2 |
Completeness [%] | 99.4 | |
Redundancy | 3.9 | |
CC(1/2) | 1.000 | 0.610 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | PEG 3350, BIS-TRIS, lithium sulfate |