PubMed · 14326070
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W GUTMAN. SILICEA.. https://pubmed.ncbi.nlm.nih.gov/14326070/
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Experiments have been carried out to study the behavior of L-threonine (needle-like) crystals during agitated drying. For an L-threonine/water system the morphology of the crystals was monitored using light microscopy and image analysis. Analysis of the transient behavior of the crystal size and shape distribution showed that attrition and agglomeration took place simultaneously during the process. The variation of the operating conditions (temperature, agitation and vacuum) revealed that attrition dominated the drying process when the drying rate was low and/or the shear rate was high. For high drying rates and low shear rates, agglomeration became dominant. This study suggests that crystal redissolution had no significant impact on crystal morphology. It was also found that due to their needle-like shape, large L-threonine crystals were very sensitive to attrition. When attrition controlled the drying process, most of the particle size reduction took place below a critical moisture content of 4%. When agglomeration controlled the drying process, most of the crystal size enlargement occurred below a moisture content of 6%.
Enantioselective crystal growth of leucine occurs on a solid surface modified with a self-assembled monolayer depending on the chirality of the enantiomer attached, as evidenced by the X-ray diffraction method.
Mitogen-activated protein (MAP) kinase p38 alpha is activated in response to environmental stress and cytokines, and plays a significant role in inflammatory responses. For these reasons, it is an important target for the treatment of a wide range of inflammatory and autoimmune diseases. The crystals of p38 alpha that we obtained by published procedures were usually small, quite mosaic, and difficult to reproduce and thus posed a difficulty for the intensive high-resolution studies required for a structure-guided drug discovery approach. Based on crystallographic and biochemical evidences, we prepared a single point mutation of a surface cysteine (C162S) and found that it prevents aggregation and improves the homogeneity and stability of the enzyme. This mutation also facilitates the crystallization process and increases the diffracting power of p38 alpha crystals. Surprisingly, we found that the mutation induces a change in the conformation of a nearby surface loop resulting in stronger lattice interactions, consistent with the improved crystal quality. The mutant protein, because of its improved stability and strengthened lattice interactions, thus provides a significantly improved reagent for use in structure-based drug design for this important disease target.