A gel can be considered to be a two-phase (liquid and solid) system, which lacks flow once it reaches a stationary state. The solid phase is usually a tridimensional polymeric mesh, while the liquid phase is usually found in three forms: contained in great cavities, retained in the capillary pores between micelles, or adsorbed on the surface of a micelle. The influence of the use of gels in crystal growth is diverse and depends on the type of gel being used. A decrease in solubility of any solute in the liquid may occur if the solvent interacts extensively with the polymeric section, hence, the nucleation in gels in these cases apparently occurs at relatively low supersaturations. However, if the pore size is small enough, there is a possibility that a higher supersaturation is needed, due to the compartmentalization of solvents. Finally, this may also represent an effect in the diffusion of substances. This review is divided into three main parts; the first evaluates the theory and practice used for the obtainment of polymorphs. The second part describes the use of gels into crystallogenesis of different substances. The last part is related to the particularities of protein crystal polymorphism, as well as modern trends in gel growth for high-resolution X-ray crystallography.

In this contribution we want to show how the intramineral proteins affect the crystal morphology of calcite crystals grown in vitro. Intramineral proteins from emu eggshells and two crocodile species were isolated, purified by ultrafast liquid chromatography, and characterized by biochemical and biophysical methods. We saw that the crystal habit of calcite was modified when intramineral proteins were present at certain concentration. Therefore, all crystal species were individually characterized by scanning electron microscopy (SEM) and by electron diffraction with an electron-reduced dosage in transmission electron microscopy. Additionally, transversal SEM micrographs of eggshells of four types of species, namely, emu, crocodile, hen, and dinosaur (70 million years old), were compared to track the changes produced by the interacting intramineral proteins. Finally, the organic sulfur content analysis of these eggshells was performed by using X-ray absorption techniques like X-ray fluorescence and X-ray absorption near-edge structure. From the analyses of the dinosaur eggshells, these X-ray absorption data showed a very characteristic organic sulfur bonding similar to that semiessential proteogenic amino acid L-cysteine, which implies that there is a possibility of having a very old intramineral protein similar to those found in emu and crocodiles.

La obtención de información estructural tridimensional de una proteína es de suma importancia en campos tan variados como la bioquímica funcional, las ciencias de materiales o biomédicas. Siendo actualmente la difracción de rayos X de monocristal el estándar de oro para la consecución de este objetivo, la obtención de dicho monocristal sigue siendo un cuello de botella desde el punto de vista práctico, y poco entendido desde el punto de vista teórico. En este artículo se revisa desde la perspectiva estructural de la proteína la forma en que los rayos X permiten obtener la información estructural y las condiciones fisicoquímicas que permiten la formación de un cristal adecuado para estos experimentos.