Issue 43, 2010
From the journal:

Chemical Communications

Total chemical synthesis and X-ray structure of kaliotoxin by racemic proteincrystallography†‡

Brad L. Pentelute,a   Kalyaneswar Mandal,a   Zachary P. Gates,a   Michael R. Sawaya,bc   Todd O. Yeatesbc  and  Stephen B. H. Kent*a  

* Corresponding authors

a Department of Chemistry, Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, USA
E-mail: skent@uchicago.edu

b Molecular Biology Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, USA

c University of California Los Angeles-United States Department of Energy Institute for Genomics and Proteomics, USA

Abstract

Here we report the total synthesis of kaliotoxin by ‘one pot’ native chemical ligation of three synthetic peptides. A racemic mixture of D- and L-kaliotoxin synthetic protein molecules gave crystals in the centrosymmetric space group P[1 with combining macron] that diffracted to atomic-resolution (0.95 Å), enabling the X-ray structure of kaliotoxin to be determined by direct methods.

Graphical abstract: Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography

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Article information

DOI
https://doi.org/10.1039/C0CC03148H
Article type
Communication
Submitted
10 Aug. 2010
Accepted
06 Sept. 2010
First published
28 Sept. 2010

Chem. Commun., 2010,46, 8174-8176

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Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography

B. L. Pentelute, K. Mandal, Z. P. Gates, M. R. Sawaya, T. O. Yeates and S. B. H. Kent, Chem. Commun., 2010, 46, 8174 DOI: 10.1039/C0CC03148H

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