X-ray diffraction data for the methylmalonate-semialdehyde dehydrogenase enzyme from the marine bacterium Oceanimonas doudoroffii. The dataset includes a complete native diffraction set collected up to 2.9 Å resolution, processed in the P21212 space group. It was produced by AMD_KOPRI and last updated in 2013.
Use Cases
- Protein structure refinement based on diffraction data up to 2.9 Å resolution
- Analysis of enzyme mechanisms in dimethyl sulfonio propionate catabolism
- Comparative structural studies of methylmalonate-semialdehyde dehydrogenase enzymes
- Model building for proteins crystallized in PEG 3350 and potassium sodium tartrate
Strengths
- A complete native diffraction dataset was collected
- Data processed in the P21212 space group with specific unit-cell parameters (a=156.7, b=160.3, c=238.9 Å)
- Phase information obtained by molecular replacement
Limitations
- Last updated 2013-09-24 00:00:00; freshness should be verified
- Column-level documentation is absent; field semantics must be inferred after download
- Row count is unknown, which may limit suitability assessment
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Recombinant protein over-expressed in Escherichia coli, crystallized, and subjected to X-ray diffraction analysis.
- Freshness
- 2013-09-24 00:00:00