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Related Concept Videos

Polymer Classification: Crystallinity01:21

Polymer Classification: Crystallinity

Unlike ionic or small covalent molecules, polymers do not form crystalline solids due to the diffusion limitations of their long-chain structures. However, polymers contain microscopic crystalline domains separated by amorphous domains.
Crystalline domains are the regions where polymer chains are aligned in an orderly manner and held together in proximity by intermolecular forces. For example, chains in the crystalline domains of polyethylene and nylon are bound together by van der Waals...
Crystal Growth: Principles of Crystallization01:25

Crystal Growth: Principles of Crystallization

Crystallization is a phase transformation process in which crystals are precipitated from a supersaturated solution or formed from other sources. During crystallization, atoms or molecules arrange themselves into a well-defined, rigid crystal lattice to minimize energy.
Initiating crystallization involves manipulating the concentration of the solute and the temperature of the solution. Since crystal growth occurs when the ratio of concentration and solubility of the solute in the solvent – the...
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
Recrystallization: Solid–Solution Equilibria01:10

Recrystallization: Solid–Solution Equilibria

Recrystallization is a purification technique used to separate impurities from solid compounds. In this technique, no chemical reactions occur. Instead, it exploits physical properties only, specifically, the solubility differences between the desired compound and impurities, either at a single temperature or at different temperatures, and under other selected conditions. The solid-solution equilibrium (solubility equilibrium) of each component in the solution represents a binary phase...
Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism01:21

Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism

Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...

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Updated: Jun 15, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Protein crystallizability.

Pawel Smialowski1, Dmitrij Frishman

  • 1MIPS & Helmholz Institute München, Martinsried, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|March 12, 2010
PubMed
Summary
This summary is machine-generated.

Computational methods can predict and improve protein crystallization, a key step in structure research. This chapter reviews tools for estimating crystallization potential, optimizing sequences, and designing screening conditions.

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Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
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Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

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Last Updated: Jun 15, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

High-Throughput Protein Crystallization via Microdialysis
06:18

High-Throughput Protein Crystallization via Microdialysis

Published on: March 3, 2023

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
09:52

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Published on: February 4, 2021

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Crystallization is crucial for determining protein structures.
  • Obtaining well-diffracting crystals is a significant bottleneck in structural biology.

Purpose of the Study:

  • To review computational methods for protein crystallization.
  • To guide optimization of protein sequences for better crystal formation.
  • To aid in designing effective crystal screening strategies.

Main Methods:

  • Review of existing computational algorithms and software.
  • Analysis of methods for predicting crystallization potential.
  • Examination of sequence optimization techniques.
  • Assessment of strategies for designing crystal screens.

Main Results:

  • Computational tools can estimate a protein's likelihood of crystallization.
  • Sequence optimization can enhance the probability of obtaining crystals.
  • In silico design can improve the efficiency of crystal screening.

Conclusions:

  • Computational approaches offer powerful solutions to crystallization challenges.
  • These methods accelerate protein structure determination.
  • Integrating computational tools is vital for modern structural biology research.