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X-ray Crystallography

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...

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Related Experiment Video

Updated: Mar 11, 2026

Protein Crystallization for X-ray Crystallography

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

A Practical Approach to Protein Crystallography.

Andrea Ilari¹, Carmelinda Savino²

¹C.N.R.-Istituto di Biologia e Patologia Molecolari c/o Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università "Sapienza", P.le Aldo Moro, 5, 00185, Rome, Italy. andrea.ilari@uniroma1.it.

Methods in Molecular Biology (Clifton, N.J.)

|November 30, 2016

Summary

This summary is machine-generated.

Determining protein crystal structures is now more accessible due to advancements in macromolecular crystallography. This guide focuses on the Molecular Replacement method for efficient structure determination using the Protein Data Bank.

Keywords:

Coordinates refinement Model building Molecular replacement Protein crystallization X-ray crystallography

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Last Updated: Mar 11, 2026

Protein Crystallization for X-ray Crystallography

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

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Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

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Published on: March 3, 2023

Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Macromolecular crystallography is a key technique in structural biology.
Advances in computing, automation, and synchrotron sources have simplified protein crystal structure determination.
The Protein Data Bank (PDB) now houses over 100,000 entries, increasing the availability of search models.

Purpose of the Study:

To provide practical procedures for determining protein crystal structures.
To highlight new techniques, experimental methods, and software in protein crystallography.
To make protein crystallography accessible to a broader scientific community.

Main Methods:

Focus on the Molecular Replacement (MR) method for structure determination.
Utilizes a search model from the Protein Data Bank (PDB).
Relies on computational analysis of a single diffraction dataset.

Main Results:

The MR method enables the resolution of macromolecular structures efficiently.
Accessibility of protein crystallography has increased significantly.
The growing PDB database enhances the success rate of MR.

Conclusions:

Macromolecular crystallography, particularly the MR method, is a powerful and increasingly accessible tool for structural biology.
The availability of extensive structural data in the PDB facilitates structure determination.
This chapter serves as a practical guide for researchers new to protein crystallography.