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

Ionic Crystal Structures02:42

Ionic Crystal Structures

17.0K
Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...
17.0K
Crystal Growth: Principles of Crystallization01:25

Crystal Growth: Principles of Crystallization

5.0K
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...
5.0K
Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

30.8K
Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
30.8K
Crystal Field Theory - Tetrahedral and Square Planar Complexes02:46

Crystal Field Theory - Tetrahedral and Square Planar Complexes

48.5K
Tetrahedral Complexes
Crystal field theory (CFT) is applicable to molecules in geometries other than octahedral. In octahedral complexes, the lobes of the dx2−y2 and dz2 orbitals point directly at the ligands. For tetrahedral complexes, the d orbitals remain in place, but with only four ligands located between the axes. None of the orbitals points directly at the tetrahedral ligands. However, the dx2−y2 and dz2 orbitals (along the Cartesian axes) overlap with the ligands less than the dxy,...
48.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.7K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
Protein and Protein Structure02:15

Protein and Protein Structure

87.6K
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...
87.6K

You might also read

Related Articles

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

Sort by
Same author

<i>Escherichia coli</i> Triheme Enzyme YhjA: Structure and Reactivity.

Biochemistry·2025
Same author

Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra.

Nature communications·2024
Same author

Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins.

Nature protocols·2024
Same author

New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.

Protein science : a publication of the Protein Society·2023
Same author

Structural consequences of turnover-induced homocitrate loss in nitrogenase.

Nature communications·2023
Same author

Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer.

Biochemistry·2022

Related Experiment Video

Updated: Feb 4, 2026

Author Spotlight: High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography
06:19

Author Spotlight: High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography

Published on: March 10, 2023

5.7K

Crystallization of Nitrogenase Proteins.

Belinda B Wenke1, Renee J Arias1, Thomas Spatzal2

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 15, 2018
PubMed
Summary

Nitrogenase enzymes convert atmospheric nitrogen to ammonia, a vital process for life. New structural insights from X-ray diffraction reveal atomic details of this complex nitrogen fixation mechanism.

Keywords:
CrystallizationFe protein (Av2)MoFe protein (Av1)NitrogenaseSingle-crystal spectroscopyX-ray diffraction (XRD)

More Related Videos

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

65.1K
High-Throughput Protein Crystallization via Microdialysis
06:18

High-Throughput Protein Crystallization via Microdialysis

Published on: March 3, 2023

3.0K

Related Experiment Videos

Last Updated: Feb 4, 2026

Author Spotlight: High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography
06:19

Author Spotlight: High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography

Published on: March 10, 2023

5.7K
Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

65.1K
High-Throughput Protein Crystallization via Microdialysis
06:18

High-Throughput Protein Crystallization via Microdialysis

Published on: March 3, 2023

3.0K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Nitrogenase is the sole enzyme system known to convert atmospheric dinitrogen (N₂) into ammonia.
  • This process is crucial for the biological nitrogen cycle but is highly sensitive to oxygen and requires significant ATP.
  • Decades of research have elucidated aspects of nitrogen fixation, yet key mechanistic steps at an atomic level are still being uncovered.

Purpose of the Study:

  • To detail protocols for crystallizing Azotobacter vinelandii (Av) nitrogenase component proteins.
  • To connect spectroscopic and functional properties with detailed three-dimensional structures.
  • To enable structural characterization of inhibitors and facilitate atomic-level mechanistic understanding.

Main Methods:

  • X-ray diffraction (XRD) for high-resolution structural determination.
  • Crystallization techniques for nitrogenase component proteins (MoFe- and Fe-proteins).
  • Single-crystal spectroscopy for functional property analysis.

Main Results:

  • Detailed three-dimensional structures of nitrogenase components have been obtained.
  • Atomic-level insights into the enzyme system, particularly the active site FeMo-cofactor, are provided.
  • Protocols for crystallization and structural characterization are outlined.

Conclusions:

  • Structural information from XRD is critical for understanding nitrogenase function.
  • Crystallization protocols enable detailed atomic analysis of nitrogen fixation.
  • Further structural studies will illuminate the intricate mechanism of N₂ reduction.