Alpha-Momorcharin Crystal Structure in Acetonitrile-Water Mixture

Peking University researchers determined the crystal structure of the ribosome-inactivating protein alpha-momorcharin (MMC) in an 80% acetonitrile-water mixture to 2.2 Å resolution. The dataset likely contains atomic coordinates and structural factors from X-ray diffraction, revealing the conformation of a sugar chain on Asn-227 that was previously undefined in aqueous systems. The work by Guangyu Zhu demonstrates conformational alterations of the tetrasaccharide in organic media.

Use Cases

• Modeling glycoprotein oligosaccharide conformation based on electron density maps from organic media.
• Studying protein-solvent interactions by comparing structures in aqueous versus low-water systems.
• Training algorithms for protein structure prediction using data from non-aqueous crystallization conditions.
• Analyzing intramolecular hydrogen bonding patterns between oligosaccharides and protein moieties.

Strengths

• X-ray data collected to a high resolution of 2.2 Å.
• Structure reveals a previously undefined sugar chain conformation on Asn-227.
• Analysis includes comparison of active center residues between organic and aqueous systems.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Guangyu Zhu, Peking University, via paperswithcode.

Collection Method

X-ray crystallography of cross-linked protein crystals soaked in an 80% acetonitrile-water mixture.