From Ions to Crystals: A Comprehensive View of the Non-Classical Nucleation of Calcium Sulfate.

The early stages of mineralization continue to be in the focus of intensive research due to their inherent importance for natural and engineered environments. While numerous observations have been reported for single steps in the pathways of various crystallizing phases in previous studies, the complexity of the underlying processes and their elusive character have left central questions unanswered in most cases. In the present work, we provide a detailed view on the nucleation of calcium sulfate mineralization-an abundant mineral with broad use in construction industry-in aqueous systems at ambient conditions.

Organic solvent-free synthesis of calcium sulfate hemihydrate at room temperature.

Calcium sulfate hemihydrate, also known as bassanite or Plaster of Paris, is one of the most extensively produced inorganic materials worldwide. Nowadays, bassanite is mainly obtained by thermal dehydration of calcium sulfate dihydrate (gypsum) - a process that consumes considerable amounts of energy and thus leaves a significant carbon footprint. Towards a more sustainable future, alternative technologies for bassanite production at low temperatures are therefore urgently required.

Evidence for liquid-liquid phase separation during the early stages of Mg-struvite formation.

The precipitation of struvite, a magnesium ammonium phosphate hexahydrate (MgNH4PO4 · 6H2O) mineral, from wastewater is a promising method for recovering phosphorous. While this process is commonly used in engineered environments, our understanding of the underlying mechanisms responsible for the formation of struvite crystals remains limited. Specifically, indirect evidence suggests the involvement of an amorphous precursor and the occurrence of multi-step processes in struvite formation, which would indicate non-classical paths of nucleation and crystallization.

Hierarchical synchrotron diffraction and imaging study of the calcium sulfate hemihydrate-gypsum transformation.

The mechanism of hydration of calcium sulfate hemihydrate (CaSO·0.5HO) to form gypsum (CaSO·2HO) was studied by combining scanning 3D X-ray diffraction (s3DXRD) and phase contrast tomography (PCT) to determine the spatial and crystallographic relationship between these two phases. From s3DXRD measurements, the crystallographic structure, orientation and position of the crystalline grains in the sample during the hydration reaction were obtained, while the PCT reconstructions allowed visualization of the 3D shapes of the crystals during the reaction.

Advanced materials engineering in historical gypsum plaster formulations.

We show how historical gypsum plaster preparation methods affect the microstructure and the wettability properties of the final stucco materials. We reproduced a traditional Persian recipe ( ~14th century AD), which involves a continuous mechanical treatment during plaster hydration. These samples were compared with a laboratory-replicated historical recipe from Renaissance Italy ( ~15th century AD) and contemporary low-strength plaster.

Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.

Protein crystallization is an astounding feat of nature. Even though proteins are large, anisotropic molecules with complex, heterogeneous surfaces, they can spontaneously group into two- and three-dimensional arrays with high precision. And yet, the biggest hurdle in this assembly process, the formation of a nucleus, is still poorly understood.

Seeds of imperfection rule the mesocrystalline disorder in natural anhydrite single crystals.

In recent years, we have come to appreciate the astounding intricacies associated with the formation of minerals from ions in aqueous solutions. In this context, a number of studies have revealed that the nucleation of calcium sulfate systems occurs nonclassically, involving the aggregation and reorganization of nanosized prenucleation species. In recent work, we have shown that this particle-mediated nucleation pathway is actually imprinted in the resultant micrometer-sized CaSO crystals.

Nucleation of protein mesocrystals via oriented attachment.

Self-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towards a desired organized state. Although proven effective, this approach poses restrictions on the complexity and material properties of the end-state.

High mobility of lattice molecules and defects during the early stage of protein crystallization.

Protein crystals are expected to be useful not only for their molecular structure analysis but also as functional materials due to their unique properties. Although the generation and the propagation of defects during crystallization play critical roles in the final properties of protein crystals, the dynamics of these processes are poorly understood. By time-resolved liquid-cell transmission electron microscopy, we observed that nanosized crystal defects are surprisingly mobile during the early stages of the crystallization of a lysozyme as a model protein.

Nucleation of protein crystals - a nanoscopic perspective.

Macromolecular phase transitions bear great medical, scientific and industrial relevance, yet the molecular picture of their earliest beginnings is still far from complete. For decades, progress has been hampered by the challenges associated with studying stochastic nucleation phenomena occurring on nanoscopic length scales. In the last 5 years, however, the field has advanced with great strides due to the recent buildout of experimental techniques that allow us to observe details of the nucleation process on the nanoscale.

Molecular nucleation mechanisms and control strategies for crystal polymorph selection.

The formation of condensed (compacted) protein phases is associated with a wide range of human disorders, such as eye cataracts, amyotrophic lateral sclerosis, sickle cell anaemia and Alzheimer's disease. However, condensed protein phases have their uses: as crystals, they are harnessed by structural biologists to elucidate protein structures, or are used as delivery vehicles for pharmaceutical applications. The physiochemical properties of crystals can vary substantially between different forms or structures ('polymorphs') of the same macromolecule, and dictate their usability in a scientific or industrial context.

Two types of amorphous protein particles facilitate crystal nucleation.

Nucleation, the primary step in crystallization, dictates the number of crystals, the distribution of their sizes, the polymorph selection, and other crucial properties of the crystal population. We used time-resolved liquid-cell transmission electron microscopy (TEM) to perform an in situ examination of the nucleation of lysozyme crystals. Our TEM images revealed that mesoscopic clusters, which are similar to those previously assumed to consist of a dense liquid and serve as nucleation precursors, are actually amorphous solid particles (ASPs) and act only as heterogeneous nucleation sites.

The Molecular Mechanism of Iron(III) Oxide Nucleation.

A molecular understanding of the formation of solid phases from solution would be beneficial for various scientific fields. However, nucleation pathways are still not fully understood, whereby the case of iron (oxyhydr)oxides poses a prime example. We show that in the prenucleation regime, thermodynamically stable solute species up to a few nanometers in size are observed, which meet the definition of prenucleation clusters.

Formation of calcium sulfate through the aggregation of sub-3 nanometre primary species.

The formation pathways of gypsum remain uncertain. Here, using truly in situ and fast time-resolved small-angle X-ray scattering, we quantify the four-stage solution-based nucleation and growth of gypsum (CaSO4·2H2O), an important mineral phase on Earth and Mars. The reaction starts through the fast formation of well-defined, primary species of <3 nm in length (stage I), followed in stage II by their arrangement into domains.

Step Crowding Effects Dampen the Stochasticity of Crystal Growth Kinetics.

Crystals grow by laying down new layers of material which can either correspond in size to the height of one unit cell (elementary steps) or multiple unit cells (macrosteps). Surprisingly, experiments have shown that macrosteps can grow under conditions of low supersaturation and high impurity density such that elementary step growth is completely arrested. We use atomistic simulations to show that this is due to two effects: the fact that the additional layers bias fluctuations in the position of the bottom layer towards growth and by a transition, as step height increases, from a 2D to a 3D nucleation mechanism.

Mesoscopic Impurities Expose a Nucleation-Limited Regime of Crystal Growth.

Nanoscale self-assembly is naturally subject to impediments at the nanoscale. The recently developed ability to follow processes at the molecular level forces us to resolve older, coarse-grained concepts in terms of their molecular mechanisms. In this Letter, we highlight one such example.

In situ observation of biotite (001) surface dissolution at pH 1 and 9.5 by advanced optical microscopy.

Laser confocal differential interference contrast microscopy (LCM-DIM) allows for the study of the reactivity of surface minerals with slow dissolution rates (e.g., phyllosilicates).

Controlling the selective formation of calcium sulfate polymorphs at room temperature.

Calcium sulfate is a naturally abundant and technologically important mineral with a broad scope of applications. However, controlling CaSO4 polymorphism and, with it, its final material properties still represents a major challenge, and to date there is no universal method for the selective production of the different hydrated and anhydrous forms under mild conditions. Herein we report the first successful synthesis of pure anhydrite from solution at room temperature.

Observing classical nucleation theory at work by monitoring phase transitions with molecular precision.

It is widely accepted that many phase transitions do not follow nucleation pathways as envisaged by the classical nucleation theory. Many substances can traverse intermediate states before arriving at the stable phase. The apparent ubiquity of multi-step nucleation has made the inverse question relevant: does multistep nucleation always dominate single-step pathways? Here we provide an explicit example of the classical nucleation mechanism for a system known to exhibit the characteristics of multi-step nucleation.

Role of clusters in nonclassical nucleation and growth of protein crystals.

The development of multistep nucleation theory has spurred on experimentalists to find intermediate metastable states that are relevant to the solidification pathway of the molecule under interest. A great deal of studies focused on characterizing the so-called "precritical clusters" that may arise in the precipitation process. However, in macromolecular systems, the role that these clusters might play in the nucleation process and in the second stage of the precipitation process, i.

Microbial diversity in the deep-subsurface hydrothermal aquifer feeding the giant gypsum crystal-bearing Naica Mine, Mexico.

The Naica Mine in northern Mexico is famous for its giant gypsum crystals, which may reach up to 11 m long and contain fluid inclusions that might have captured microorganisms during their formation. These crystals formed under particularly stable geochemical conditions in cavities filled by low salinity hydrothermal water at 54-58°C. We have explored the microbial diversity associated to these deep, saline hydrothermal waters collected in the deepest (ca.

Does Solution Viscosity Scale the Rate of Aggregation of Folded Proteins?

Viscosity effects on the kinetics of complex solution processes have proven hard to predict. To test the viscosity effects on protein aggregation, we use the crystallization of the protein glucose isomerase (gluci) as a model and employ scanning confocal and atomic force microscopies at molecular resolution, dynamic and static light scattering, and rheometry. We add glycerol to vary solvent viscosity and demonstrate that glycerol effects on the activation barrier for attachment of molecules to the crystal growth sites are minimal.

In situ observation of elementary growth processes of protein crystals by advanced optical microscopy.

To start systematically investigating the quality improvement of protein crystals, the elementary growth processes of protein crystals must be first clarified comprehensively. Atomic force microscopy (AFM) has made a tremendous contribution toward elucidating the elementary growth processes of protein crystals and has confirmed that protein crystals grow layer by layer utilizing kinks on steps, as in the case of inorganic and low-molecular-weight compound crystals. However, the scanning of the AFM cantilever greatly disturbs the concentration distribution and solution flow in the vicinity of growing protein crystals.