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

2-D Crystallization of the Rhodococcus 20S Proteasome

Aoyama¹, Zuhl, Tamura

¹Max-Planck-Institut fur Biochemie, Martinsried bei Munchen, 82152, Germany

Journal of Structural Biology

|May 1, 1996

Summary

This summary is machine-generated.

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

Invited response

Archives of surgery (Chicago, Ill. : 1960)·2001

Same author

Regiochemistry in aryl radical cyclization onto methylenecycloalkanes

The Journal of organic chemistry·2001

Same author

A Case of Multiple Juvenile Papillomatosis of the Breast and Its Immunohistochemical Pathology.

Breast cancer (Tokyo, Japan)·2000

Same author

Computer-Aided Diagnosis (CAD) for Mammography: Preliminary Results.

Breast cancer (Tokyo, Japan)·2000

Same author

The Relationship between Urinary Pyridinoline, Deoxypyridinoline and Bone Metastasis in a Rat Breast Cancer Model.

Breast cancer (Tokyo, Japan)·2000

Same author

Giant Artificial Ion Channels Formed by Self-Assembled, Cationic Rigid-Rod beta-Barrels We thank Dr. E. Buck (Warner Instrument Corp., Hamden, CT) and R. Marclay (University of Geneva) for installation of a BLM workstation, Dr. E. Buck for BLM instructions, A. Pinto, J.-P. Saulnier, the group of Prof. Gülaçar, and Dr. H. Eder for NMR, MS, and elemental analyses, respectively (University of Geneva), and the Swiss NSF and Suntory Institute for Bioorganic Research (SUNBOR Grant) for financial support.

Angewandte Chemie (International ed. in English)·2000

Researchers crystallized the Rhodococcus 20S proteasome using a liquid-liquid interface method. This yielded two ordered arrays, one with rotational freedom and a true crystal enabling 1.8 nm resolution analysis.

Area of Science:

Structural Biology
Biochemistry
Crystallography

Background:

The 20S proteasome is a crucial protein complex involved in cellular protein degradation.
High-resolution structural data of the Rhodococcus 20S proteasome is essential for understanding its function.

Purpose of the Study:

To apply a 2D crystallization method at a liquid-liquid interface to the Rhodococcus 20S proteasome.
To obtain ordered arrays suitable for high-resolution structural analysis.

Main Methods:

Utilized a 2D crystallization technique at a liquid-liquid interface.
Employed real-space correlation averaging for image analysis.
Applied an unbending procedure to enhance diffraction data.

Main Results:

Related Experiment Videos

Obtained two types of ordered arrays: a hexagonal close-packed array with rotational freedom and a true crystal with p4 symmetry.
The true crystal exhibited lattice constants a = b = 20.0 nm, with two proteasomes per unit cell.
Achieved a resolution of 1.8 nm after applying an unbending procedure to the diffraction data.

Conclusions:

The liquid-liquid interface 2D crystallization method is effective for the Rhodococcus 20S proteasome.
The obtained crystal structure provides high-resolution insights into the proteasome's molecular arrangement.
The study demonstrates a pathway to achieve near-atomic resolution for large protein complexes.