What is the impact of a lower resolution in X-ray crystallography?

Lower resolution in X-ray crystallography results in decreased clarity of the structural model because it reflects a lack of fine detail in the obtained data. In crystallography, resolution is a measure of the smallest distance between two points that can be distinguished as separate entities. When the resolution is low, the data collected is less precise, which means that the positions of atoms within the protein structure cannot be determined as accurately.

In practical terms, low resolution can cause overlapping electron density regions in the structure, making it difficult to pinpoint specific atomic positions and affecting the overall interpretation. This can lead to ambiguities in the model, resulting in a less reliable representation of the actual molecular structure. Therefore, higher resolution is critical for producing clearer and more accurate models of protein structures, enabling better understanding and insights into their functions and interactions.