6DBB
Crystal structure of a Putative aldehyde dehydrogenase family protein Burkholderia cenocepacia J2315 in complex with partially reduced NADH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-04-05 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 110.670, 124.980, 246.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.813 - 2.100 |
R-factor | 0.1479 |
Rwork | 0.147 |
R-free | 0.18930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Model identified with SIMBAD MR done with 4pxnA as per MoRDa |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SIMBAD |
Refinement software | PHENIX ((dev_3092)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.813 | 45.813 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.082 | 0.031 | 0.507 |
Rmeas | 0.092 | 0.036 | 0.566 |
Number of reflections | 99329 | 1207 | 7309 |
<I/σ(I)> | 12.78 | 28.4 | 3.08 |
Completeness [%] | 99.8 | 97.3 | 100 |
Redundancy | 4.898 | 4.17 | 5.062 |
CC(1/2) | 0.997 | 0.998 | 0.863 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | Molecular Dimensions Morpheus screen, H2: 10% PEG 8000, 20% EG: 20mM of each amino acid: sodium L-glutamate, DL-alanine, glycine, DL-lysine HCl, DL-serine: 100mM MES / Imidazole pH 6.5: BuceA.00020.r.B1.PW37259 at 20mg/ml + 2.5mM NAD: cryo: direct: tray 299802h2: puck bit3-4 |