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Related Concept Videos

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...
X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Updated: Jul 4, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Protein structure determination by x-ray crystallography.

Andrea Ilari1, Carmelinda Savino

  • 1CNR Institute of Molecular Biology and Pathology (IBPM), Department of Biochemical Sciences, University of Rome, Sapienza,, Roma, Italy.

Methods in Molecular Biology (Clifton, N.J.)
|June 20, 2008
PubMed
Summary
This summary is machine-generated.

X-ray biocrystallography is a powerful technique for determining macromolecular structures. This guide focuses on the Molecular Replacement method, simplifying the process using computational tools and existing protein data bank models.

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Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • X-ray biocrystallography is the premier method for elucidating macromolecular structures.
  • Advancements in computational technology and software have streamlined structure determination.
  • The Protein Data Bank (PDB) offers a vast repository of existing protein structures.

Purpose of the Study:

  • To provide practical guidance for solving new macromolecular structures.
  • To focus on the Molecular Replacement (MR) method for structure resolution.
  • To highlight the utility of MR in simplifying the crystallographic process.

Main Methods:

  • Utilizing X-ray biocrystallography techniques.
  • Employing computational technologies and specialized software.
  • Applying the Molecular Replacement method with a PDB search model.

Main Results:

  • The Molecular Replacement method facilitates structure resolution from a single dataset.
  • This approach leverages existing models from the Protein Data Bank.
  • Computer-aided analysis is central to the MR method's success.

Conclusions:

  • The Molecular Replacement method offers an efficient pathway to determine macromolecular structures.
  • Integration of computational tools and PDB data simplifies structure resolution.
  • X-ray biocrystallography, particularly with MR, is becoming more accessible for new structure determination.