Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
Inductively Coupled Plasma Atomic Emission Spectroscopy: Instrumentation01:26

Inductively Coupled Plasma Atomic Emission Spectroscopy: Instrumentation

Inductively coupled plasma (ICP) is the common plasma source used in atomic emission spectroscopy (AES), a technique that detects and analyzes various elements in a sample. This method is often called inductively coupled plasma atomic emission spectroscopy (ICP-AES).
There are three main types of inductively coupled plasma atomic emission spectroscopy  (ICP-AES) instruments: sequential, simultaneous multichannel, and Fourier transform instruments, with the latter being less commonly used.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structural Profiling of Lipid Nanoparticles at Sub-10 nm Resolution via AF4 Coupled Online to SAXS and SANS.

Small methods·2026
Same author

Nanodiscs formation process studied by contrast variation-SANS.

Biochimica et biophysica acta. Biomembranes·2026
Same author

Toward Nanodisc Tailoring for SANS Study of Membrane Proteins.

Bioengineering (Basel, Switzerland)·2026
Same author

pH-triggered clustering regulates β-sheet activation in silk assembly.

Communications chemistry·2026
Same author

Global Characterization of Commercial Generation 0-7 Poly(amidoamine) Dendrimers: Challenges and Opportunities for Analysis.

ACS omega·2025
Same author

Comprehensive Analysis of Interactions between Human Serum Albumin and Human Cystatin C - Two Proteins Present in Body Fluids.

ACS omega·2025

Related Experiment Video

Updated: May 23, 2026

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution
12:53

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

An integrated high-throughput data acquisition system for biological solution X-ray scattering studies.

Anne Martel1, Ping Liu, Thomas M Weiss

  • 1Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.

Journal of Synchrotron Radiation
|April 20, 2012
PubMed
Summary

A new automated system enhances high-throughput protein structure studies using X-ray scattering. This advanced solution X-ray scattering (SXS) system offers rapid, reliable data collection with minimal sample volume and high accuracy.

More Related Videos

User-friendly, High-throughput, and Fully Automated Data Acquisition Software for Single-particle Cryo-electron Microscopy
07:56

User-friendly, High-throughput, and Fully Automated Data Acquisition Software for Single-particle Cryo-electron Microscopy

Published on: July 29, 2021

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Related Experiment Videos

Last Updated: May 23, 2026

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution
12:53

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

User-friendly, High-throughput, and Fully Automated Data Acquisition Software for Single-particle Cryo-electron Microscopy
07:56

User-friendly, High-throughput, and Fully Automated Data Acquisition Software for Single-particle Cryo-electron Microscopy

Published on: July 29, 2021

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Protein structure determination is crucial for understanding biological function.
  • Traditional X-ray scattering methods can be time-consuming and require significant sample volumes.
  • High-throughput methods are needed to accelerate structural biology research.

Purpose of the Study:

  • To develop and implement a fully automated high-throughput solution X-ray scattering (SXS) data collection system.
  • To improve the efficiency and reliability of SXS experiments for protein structure studies.
  • To integrate sample delivery, data collection, and data processing for seamless workflow.

Main Methods:

  • Development of an automated system using a quartz capillary cell, XYZ positioning arm, and computer-controlled fluid dispenser.
  • Integration with Blu-Ice/DCS beamline control software for intuitive operation.
  • In situ UV absorption spectrometer for spectrophotometric determination of protein concentration.
  • Automated data processing program for customized data collection strategies.

Main Results:

  • The system enables rapid data collection, with each measurement taking approximately 3.5 minutes, including capillary cleaning.
  • Requires only 20-30 µl of sample per measurement.
  • Achieved over 98.5% valid measurements, significantly reducing artefacts like air bubbles.
  • The compact sample changer allows easy integration with other experimental setups.

Conclusions:

  • The developed automated SXS system significantly enhances throughput and efficiency for protein structure studies.
  • The system provides a robust and user-friendly platform for collecting high-quality scattering data.
  • This automation facilitates faster structural biology research and drug discovery efforts.