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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...
Super-resolution Fluorescence Microscopy01:37

Super-resolution Fluorescence Microscopy

Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been developed.

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Related Experiment Video

Updated: Jun 2, 2026

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Acoustically mounted microcrystals yield high-resolution X-ray structures.

Alexei S Soares1, Matthew A Engel, Richard Stearns

  • 1Biology Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA. soares@bnl.gov

Biochemistry
|May 6, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a novel method for determining crystal structures using X-ray diffraction on microcrystal samples. The technique enables high-resolution structure determination from tiny amounts of material.

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A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

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Last Updated: Jun 2, 2026

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline
09:00

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

Published on: June 17, 2021

Area of Science:

  • Structural biology
  • Crystallography
  • Biophysics

Background:

  • Determining the structure of biological macromolecules is crucial for understanding their function.
  • Traditional methods often require large, well-ordered crystals, which are difficult to obtain for many important biological targets.
  • Microcrystal analysis offers a potential alternative for challenging samples.

Purpose of the Study:

  • To develop a general strategy for determining crystal structures from microcrystal samples.
  • To enable high-resolution structure determination from small amounts of material.
  • To overcome limitations of traditional crystallography.

Main Methods:

  • Utilizing acoustic droplet ejection to transfer microcrystal slurries.
  • Employing X-ray diffraction with a micro-focused X-ray beam.
  • Raster-scanning micromeshes to locate individual microcrystals.
  • Merging diffraction data from multiple microcrystals.

Main Results:

  • Demonstrated a general strategy for microcrystal structure determination.
  • Achieved 1.8 Å resolution crystal structures.
  • Successfully transferred microcrystals using acoustic droplet ejection.
  • Located individual microcrystals via X-ray raster-scanning.

Conclusions:

  • The developed method provides a powerful new approach for solving crystal structures.
  • This technique expands the possibilities for structural analysis of challenging biological samples.
  • The strategy is applicable to determining high-resolution structures from microcrystal showers.