Protein crystallography refinement is a critical step in the process of determining the three-dimensional structure of proteins at atomic resolution. This process involves adjusting the initial model of the protein's structure to minimize the differences between the observed diffraction data and the calculated structure factors. The refinement is typically conducted using methods such as least-squares fitting and maximum likelihood estimation, which iteratively improve the model parameters, including atomic positions and thermal factors.
During this phase, several factors are considered to achieve an optimal fit, including geometric constraints (like bond lengths and angles) and chemical properties of the amino acids. The refinement process is essential for achieving a low R-factor, which is a measure of the agreement between the observed and calculated data, typically expressed as:
where represents the observed structure factors and the calculated structure factors. Ultimately, successful refinement leads to a high-quality model that can provide insights into the protein's function and interactions.
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