Issue 22, 2012
From the journal:

Chemical Communications

The crystal structure of l-arginine†

Emilie Courvoisier,ab   P. Andrew Williams,a   Gin Keat Lim,a   Colan E. Hughesa  and  Kenneth D. M. Harris*a  

* Corresponding authors

a School of Chemistry, Cardiff University, Park Place, Cardiff CF10 3AT, Wales, UK
E-mail: HarrisKDM@cardiff.ac.uk

b Ecole Nationale Supérieure de Chimie de Clermont-Ferrand, Ensemble Scientifique des Cézeaux, 24 Avenue des Landais - BP 187, Aubière Cedex, France

Abstract

We report the crystal structure of L-arginine, one of the last remaining natural amino acids for which the crystal structure has never been determined; structure determination was carried out directly from powder X-ray diffraction (XRD) data, exploiting the direct-space genetic algorithm technique for structure solution followed by Rietveld refinement.

Graphical abstract: The crystal structure of l-arginine

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C2CC17203H
Article type
Communication
Submitted
19 Nov 2011
Accepted
09 Jan 2012
First published
12 Jan 2012

Chem. Commun., 2012,48, 2761-2763

Permissions

Request permissions

The crystal structure of L-arginine

E. Courvoisier, P. A. Williams, G. K. Lim, C. E. Hughes and K. D. M. Harris, Chem. Commun., 2012, 48, 2761 DOI: 10.1039/C2CC17203H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements