Crystal screening for protein crystallization
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Protein Crystalization Screening - Case Study

Crystal screening is an important process in the determination of protein structures. Proteins are crystallized in order to determine their molecular structure by x-ray protein crystallography. However, the most time consuming process on the path to determining molecular structure is the protein crystallization step. This involves crystal screening a large number of buffer conditions until conditions are ideal to induce protein crystal growth.

In general terms:

Low polydispersity is good, high polydispersity is bad for high quality crystal growth.

It was found that results from light scattering instrumentation can be used to simplify the determination of the protein crystallization process. Light scattering may be used to screen protein samples quickly and with very little sample required.

 
  
Presentations:
 
 
On demand presentation on Protein Crystaliztion Screening.
In protein structure determination x-ray protein crystallography is still the best tool available today. The bottleneck in determining protein structure remains the actual protein crystallization step and more specifically, the search for the optimum protein crystallization condition. Random screens of buffers are often applied to find a hit or narrow the search area. A different approach involves the measurement of the solvent-protein interactions via the second virial coefficient. If this parameter falls into a narrow “crystallization slot” conditions are ideal. However, this is time consuming. A faster snapshot of the protein in solution is obtained with dynamic light scattering. The width of the size distribution (polydispersity) is related to the chance of protein crystallization success. DLS provides a fast, non-invasive, low volume, sensitive screening technique for assessing crystallizability of protein solutions.