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Volume 69 
Part 5 
Page o643  
May 2013  

Received 18 March 2013
Accepted 26 March 2013
Online 5 April 2013

Key indicators
Single-crystal X-ray study
T = 308 K
Mean [sigma](C-C) = 0.002 Å
R = 0.037
wR = 0.114
Data-to-parameter ratio = 32.9
Details
Open access

rac-5-(1-Methylethyl)-2-sulfanylideneimidazolidin-4-one

aInstituto de Física - UFG, Caixa Postal 131, 74001-970 Goiânia, GO, Brazil,bDepartamento de Química - UEL, Caixa Postal 6001, 86051-990 Londrina, PR, Brazil, and cDepartamento de Química - UFMG, 31270-901 - Belo Horizonte, MG, Brazil
Correspondence e-mail: rosanepc@posgrad.ufg.br

In the title compound, C6H10N2OS, the 2-sulfanylideneimidazolidin-4-one fragment is essentially planar (r.m.s. deviation = 0.0033 Å). In the crystal, one amino group is involved in N-H...O hydrogen bonding, which links pairs of molecules into inversion dimers, while the other amino group generates weak N-H...S hydrogen bonds, which link these dimers into chains in [10-1]. The chains are further aggregated into layers parallel to the ac plane through weak C-H...O interactions.

Related literature

For the biological activity of 2-thiohydantoin derivatives, see: Ghoneim et al. (1987[Ghoneim, K. M., El-Telbany, F. & Ismail, M. A. (1987). Egypt. J. Pharm. Sci. 28, 77-86.]); Marton et al. (1993[Marton, J., Enisz, J., Hosztafi, S. & Timar, T. (1993). J. Agric. Food Chem. 41, 148-152.]). For the crystal structures of related compounds, see: Kunimoto et al. (2009[Kunimoto, K.-K., Ichitani, M., Ogawa, T., Kitoh, S.-I., Kuwae, A. & Hanai, K. (2009). Spectrosc. Lett. 42, 73-80.]); Ogawa et al. (2007[Ogawa, T., Kitoh, S.-I., Ichitani, M., Kuwae, A., Hanai, K. & Kunimoto, K.-K. (2007). Anal. Sci. X-Ray Struct. Anal. Online, 42, x199-x200.]). For details of the synthesis, see: Wang et al. (2006[Wang, Z. D., Sheikh, S. O. & Zhang, Y. (2006). Molecules, 11, 739-750.]).

[Scheme 1]

Experimental

Crystal data
  • C6H10N2OS

  • Mr = 158.23

  • Monoclinic, P 21 /c

  • a = 5.7161 (1) Å

  • b = 17.4091 (4) Å

  • c = 8.2505 (2) Å

  • [beta] = 103.513 (1)°

  • V = 798.30 (3) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.34 mm-1

  • T = 308 K

  • 0.93 × 0.4 × 0.3 mm

Data collection
  • Bruker APEXII CCD diffractometer

  • Absorption correction: multi-scan (SADABS; Bruker, 2010[Bruker (2010). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]) Tmin = 0.936, Tmax = 0.979

  • 18741 measured reflections

  • 3064 independent reflections

  • 2544 reflections with I > 2[sigma](I)

  • Rint = 0.020

Refinement
  • R[F2 > 2[sigma](F2)] = 0.037

  • wR(F2) = 0.114

  • S = 1.02

  • 3064 reflections

  • 93 parameters

  • H-atom parameters constrained

  • [Delta][rho]max = 0.33 e Å-3

  • [Delta][rho]min = -0.20 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N2-H2...O1i 0.86 2.02 2.8573 (11) 164
N1-H1...S1ii 0.86 2.52 3.3806 (9) 176
C6-H6C...O1iii 0.96 2.52 3.4434 (14) 160
Symmetry codes: (i) -x, -y+1, -z+1; (ii) -x+1, -y+1, -z; (iii) x+1, y, z.

Data collection: APEX2 (Bruker, 2010[Bruker (2010). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]); cell refinement: SAINT (Bruker, 2010[Bruker (2010). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]); data reduction: SAINT; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: ORTEP-3 for Windows (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]); software used to prepare material for publication: WinGX (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: CV5395 ).


Acknowledgements

This work includes part of the activities developed by the Network of Studies and the Development of Novel Inhibitors of Urease, financed by CNPq (562479/2010-4) and FAPEMIG (APQ-04781-10). The authors are also grateful to CNPq (TOB) and CAPES (RPC) for providing their respective fellowships.

References

Bruker (2010). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.
Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.  [ISI] [CrossRef] [ChemPort] [details]
Ghoneim, K. M., El-Telbany, F. & Ismail, M. A. (1987). Egypt. J. Pharm. Sci. 28, 77-86.  [ChemPort]
Kunimoto, K.-K., Ichitani, M., Ogawa, T., Kitoh, S.-I., Kuwae, A. & Hanai, K. (2009). Spectrosc. Lett. 42, 73-80.  [ISI] [CSD] [CrossRef] [ChemPort]
Marton, J., Enisz, J., Hosztafi, S. & Timar, T. (1993). J. Agric. Food Chem. 41, 148-152.  [CrossRef] [ChemPort] [ISI]
Ogawa, T., Kitoh, S.-I., Ichitani, M., Kuwae, A., Hanai, K. & Kunimoto, K.-K. (2007). Anal. Sci. X-Ray Struct. Anal. Online, 42, x199-x200.  [CSD] [CrossRef]
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [ChemPort] [details]
Wang, Z. D., Sheikh, S. O. & Zhang, Y. (2006). Molecules, 11, 739-750.  [CrossRef] [PubMed] [ChemPort]


Acta Cryst (2013). E69, o643  [ doi:10.1107/S1600536813008337 ]

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