Pseudomonas fluorescens Isocyanide Hydratase Mutant Structural and Kinetic Data

Experimental data from time-resolved mix-and-inject serial crystallography, ambient-temperature X-ray crystallography, computer simulations, and enzyme kinetics. The dataset characterizes how covalent catalysis modulates isocyanide hydratase conformational dynamics throughout its catalytic cycle, including a Gly150A mutant. It was produced by M.A. Wilson at the University of Nebraska–Lincoln.

Use Cases

• Modeling enzyme reaction mechanisms based on observed thioimidate covalent intermediate formation.
• Analyzing the relationship between helical mobility and catalytic efficiency based on Gly150 mutant kinetic behavior.
• Studying catalysis-activated protein motions based on described hydrogen bond strength changes and water entry into the active site.

Strengths

• Data integrates multiple experimental techniques: XFEL-based MISC, ambient-temperature crystallography, simulations, and kinetics.
• Directly visualizes a previously hypothetical reaction mechanism, capturing formation of a thioimidate covalent intermediate.

Limitations

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

Provenance

Source

University of Nebraska–Lincoln

Collection Method

Time-resolved mix-and-inject serial crystallography (MISC) at an XFEL, ambient-temperature X-ray crystallography, computer simulations, and enzyme kinetics.