Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Crystallization of Acanthamoeba profilin-I.

K A Magnus, E E Lattman, M Sato

The Journal of Biological Chemistry

|October 5, 1986

Summary

Profilin-I, a protein inhibiting actin polymerization, has been crystallized for high-resolution X-ray analysis. This structural study provides insights into Acanthamoeba castellanii profilin-I

Related Concept Videos

You might also read

Related Articles

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

Sort by

Same author

The linac coherent light source single particle imaging road map.

Structural dynamics (Melville, N.Y.)·2016

Same author

Molecular structures from femtosecond x-ray pulses.

Proceedings of the National Academy of Sciences of the United States of America·2001

Same author

Editorial on molecular dynamics simulations.

Proteins·2001

Same author

High apparent dielectric constants in the interior of a protein reflect water penetration.

Biophysical journal·2000

Same author

The duplication of an eight-residue helical stretch in Staphylococcal nuclease is not helical: a model for evolutionary change.

Proteins·2000

Same author

Crystal structure of a conserved ribosomal protein-RNA complex.

Science (New York, N.Y.)·1999

Area of Science:

Biochemistry
Structural Biology
Crystallography

Background:

Profilin-I is a protein known to inhibit actin polymerization.
Understanding protein structure is crucial for elucidating biological function.

Purpose of the Study:

To crystallize profilin-I from Acanthamoeba castellanii for high-resolution X-ray analysis.
To determine the structural characteristics of profilin-I.

Main Methods:

Protein crystallization of profilin-I.
High-resolution X-ray diffraction analysis.
Space group and lattice constant determination.

Main Results:

Profilin-I crystals were obtained, suitable for X-ray analysis.
The crystals belong to space group C2 with specific lattice constants.
Diffraction data extended to at least 2.0-Å resolution.
The asymmetric unit contains a single 12,800-dalton profilin-I monomer.

Conclusions:

The successful crystallization of profilin-I enables detailed structural studies.
These findings lay the groundwork for understanding profilin-I's mechanism of actin inhibition at a molecular level.

Related Experiment Videos