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Issue 9, 2010
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Low temperature/high pressure polymorphism in dl-cysteine

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We compare the response of the crystalline DL-cysteine to cooling and to increasing pressure. The structure undergoes a low-temperature phase transition into an isosymmetric polymorph, DL-cysteine-II, with the conformation of zwitterion changing from gauche− to gauche+. The first pressure-induced transition at 0.1 GPa (the lowest pressure reported for a phase transition in a crystalline amino acid thus far) gives the same polymorph. Further compression of DL-cysteine-II proceeds differently on cooling and with increasing hydrostatic pressure. DL-cysteine-II is preserved down to 3 K, but undergoes phase transitions on compression at about 1.55 GPa, and 6.20 GPa. The changes in the hydrogen bond network preceding the phase transition in DL-cysteine-II in the range 0.25–0.85 GPa differ from those observed on cooling the same structure, but resemble those preceding pressure-induced phase transitions in β- and γ-glycine.

Graphical abstract: Low temperature/high pressure polymorphism in dl-cysteine

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Article information

24 Feb 2010
21 Apr 2010
First published
24 May 2010

CrystEngComm, 2010,12, 2551-2560
Article type

Low temperature/high pressure polymorphism in DL-cysteine

V. S. Minkov, N. A. Tumanov, R. Q. Cabrera and E. V. Boldyreva, CrystEngComm, 2010, 12, 2551
DOI: 10.1039/C003617J

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