Technologies are described for methods and systems effective for flex plates. The flex plates may comprise a base plate. The base plate may include walls that define an insert location opening in the base plate. The insert location opening in the base plate may be in communication with a securement area. The flex plates may comprise an insert. The insert may include a reservoir region and a crystallization region separated by a wall including channels. The reservoir region and the crystallization region may include a backing. The insert may further include securement tabs. The securement tabs may be configured to secure the insert to the base plate at the securement area.

Crystal nucleation, and associated articles, systems, and methods, are generally described.

The present invention relates to an amphiphilic compound having a dendronic hydrophobic group, a method for preparing the same, and a method for extraction, solubilization, stabilization, or crystallization of a membrane protein by using the same. The use of the compound according to the present invention leads to an excellent membrane protein solubilization effect and a stable storage of a membrane protein in an aqueous solution for a long time, and thus can be utilized for functional analysis and structural analysis of the membrane protein. Especially, the amphiphilic compound having a dendronic hydrophobic group showed very remarkable characteristics in the visualization of protein composites through an electronic microscope. The membrane protein structural and functional analysis is one of the fields of greatest interest in current biology and chemistry, and more than half of the new drugs that are currently being developed are targeted at membrane proteins, and thus the amphiphilic compound of the present invention can be applied to membrane protein structure studies closely related to the development of new drugs.

Methods are disclosed for producing highly purified recombinant human insulin (RHI) having a purity of 99.0% (w/w) or greater, a Total Impurity (not including the related substance desamido Asn.sup.A21-RHI, as specified by USP) of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less. Also disclosed are API compositions of highly purified RHI having a purity of 99.0% (w/w) or greater, a Total Impurity of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less.

A method for self-assembly of a protein in a three-dimensional honeycomb structure, comprising the following consecutive steps: providing a solution comprising a solvent and a protein, the protein comprising a sequence of amino acids corresponding to an oligomerisation domain of a LEAFY protein, for example to the oligomerisation domain of Ginkgo biloba, in fusion with a tag, placing the solution in contact with a substrate, evaporating the solvent in order to crystallise the protein, the oligomerisation domain crystallising in the form of a primary helix, each primary helix interacting with six other primary helixes, whereby a three-dimensional honeycomb protein structure is obtained perpendicular to the substrate, the protein structure being attached to the substrate by the tag.

A balanced-lattice-ledge nucleant having ledge inducing local densification of proteins and a balanced-lattice inducing self-organized crystal packing. Using this balanced-lattice-ledge nucleant enhances nucleation of protein crystals.

The present invention describes the integration of preparative crystallization, crystal separation, crystal washing and freeze-drying processes of insulin and insulin analogues into single continuous process using pressure filtration. The process facilitates time reduction and outlines the novel design of using multiple organic solvent washes and nitrogen gas purging for the removal of imbibed water and achieve final drug substance that meets the quality specifications.

A crystallization method for making high-quality molecular crystals containing complexes of diacylglycerol (DAG)-effector proteins and ligands thereof. For example, some of such crystals are of a quality sufficient for crystal-structure determination by X-ray crystallography with a spatial resolution of at least 3.0 Å or, in some cases, of about 1 Å. At least some embodiments of the crystallization method and of the molecular crystals produced thereby can beneficially be used, e.g., to provide high-resolution guides for the design and development of exogenous agonists of DAG-effector proteins of therapeutic interest.

Aspects of the present application relates to co-crystal of carfilzomib with maleic acid, process for the preparation of co-crystal of carfilzomib with maleic acid, process for the preparation of pure carfilzomib from co-crystal of carfilzomib with maleic acid and process for the preparation of amorphous carfilzomib.

Disclosed are two novel crystalline forms of S-acetyl glutathione (SAG) called Form A and Form B, obtained by crystallization of SAG from mixtures of water-acetone, water-ethanol or water acetone under controlled conditions. Forms A and B can be advantageously used as ingredients of pharmaceutical or nutraceutical formulations.