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Volume 68 
Part 12 
Page o3486  
December 2012  

Received 22 November 2012
Accepted 26 November 2012
Online 30 November 2012

Key indicators
Single-crystal X-ray study
T = 100 K
Mean [sigma](C-C) = 0.002 Å
R = 0.042
wR = 0.113
Data-to-parameter ratio = 20.0
Details
Open access

1-[(1-Methyl-1H-imidazol-5-yl)methyl]-1H-indole-5-carbonitrile

aDepartment of Chemistry and Polymer Science, Stellenbosch University, Private Bag X1, Matieland 7602, South Africa
Correspondence e-mail: jjdj@sun.ac.za

In the title compound, C14H12N4, the dihedral angle between the indole ring system (r.m.s. deviation = 0.010 Å) and the imidazole ring is 77.70 (6)°. In the crystal, molecules are linked by C-H...N hydrogen bonds. One set of hydrogen bonds forms an undulating chain running parallel to the b-axis direction, while the other undulating chain is parallel to the c-axis direction. In combination, (100) sheets result.

Related literature

For background to farnesyl transferase, see: Chakrabarti et al. (2002[Chakrabarti, D., Da Silva, T., Barger, J., Paquette, S., Patel, H., Patterson, S. & Allen, C. M. (2002). J. Biol. Chem. 277, 42066-42073.]). For the properties of related compounds, see: Bulbule et al. (2008[Bulbule, V. J., Rivas, K., Verlinde, C. L. M. J., Van Voorhis, W. C. & Gelb, M. H. (2008). J. Med. Chem. 51, 384-387.]), van Voorhis et al. (2007[Voorhis, W. C. van, Rivas, K. L., Bendale, P., Nallan, L., Horney, C., Barrett, L. K., Bauer, K. D., Smart, B. P., Ankala, S., Hucke, O., Verlinde, C. L. M. J., Chakrabart, D., Strickland, C., Yokoyama, K., Buckner, F. S., Hamilton, A. D., Williams, D. K., Lombardo, L. J., Floyd, D. & Gelb, H. (2007). Antimicrob. Agents Chemother. 51, 3659-3671.]); de Ruyck & Wouters (2008[Ruyck, J. de & Wouters, J. (2008). Curr. Protein Pept. Sci. 9, 117-137.]).

[Scheme 1]

Experimental

Crystal data
  • C14H12N4

  • Mr = 236.28

  • Monoclinic, P 21 /n

  • a = 10.9624 (16) Å

  • b = 7.8687 (12) Å

  • c = 14.292 (2) Å

  • [beta] = 106.727 (2)°

  • V = 1180.6 (3) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.08 mm-1

  • T = 100 K

  • 0.10 × 0.10 × 0.02 mm

Data collection
  • Bruker APEXII CCD diffractometer

  • Absorption correction: multi-scan (SADABS; Bruker, 2009[Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]) Tmin = 0.992, Tmax = 0.998

  • 36857 measured reflections

  • 3286 independent reflections

  • 2643 reflections with I > 2[sigma](I)

  • Rint = 0.042

Refinement
  • R[F2 > 2[sigma](F2)] = 0.042

  • wR(F2) = 0.113

  • S = 1.06

  • 3286 reflections

  • 164 parameters

  • H-atom parameters constrained

  • [Delta][rho]max = 0.32 e Å-3

  • [Delta][rho]min = -0.21 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
C4-H4...N4i 0.95 2.53 3.4588 (18) 167
C13-H13...N4ii 0.95 2.57 3.4010 (18) 147
Symmetry codes: (i) [-x+{\script{3\over 2}}, y+{\script{1\over 2}}, -z+{\script{1\over 2}}]; (ii) [-x+{\script{5\over 2}}, y+{\script{1\over 2}}, -z+{\script{1\over 2}}].

Data collection: APEX2 (Bruker, 2009[Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]); cell refinement: SAINT (Bruker, 2009[Bruker (2009). 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: X-SEED (Barbour, 2001[Barbour, L. J. (2001). Supramol. Chem. 1, 189-191.]; Atwood et al., 2003[Atwood, J. L. & Barbour, L. J. (2003). Cryst. Growth Des. 3, 3-8.]); software used to prepare material for publication: SHELXL97.


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: HB7000 ).


Acknowledgements

The authors wish to thank W. A. L. van Otterlo, S. C. Pelly and the National Research Foundation for financial assistance and academic guidance.

References

Atwood, J. L. & Barbour, L. J. (2003). Cryst. Growth Des. 3, 3-8.  [CrossRef] [ChemPort]
Barbour, L. J. (2001). Supramol. Chem. 1, 189-191.  [ChemPort]
Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.
Bulbule, V. J., Rivas, K., Verlinde, C. L. M. J., Van Voorhis, W. C. & Gelb, M. H. (2008). J. Med. Chem. 51, 384-387.  [CrossRef] [PubMed] [ChemPort]
Chakrabarti, D., Da Silva, T., Barger, J., Paquette, S., Patel, H., Patterson, S. & Allen, C. M. (2002). J. Biol. Chem. 277, 42066-42073.  [CrossRef] [PubMed] [ChemPort]
Ruyck, J. de & Wouters, J. (2008). Curr. Protein Pept. Sci. 9, 117-137.  [CrossRef] [PubMed]
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Voorhis, W. C. van, Rivas, K. L., Bendale, P., Nallan, L., Horney, C., Barrett, L. K., Bauer, K. D., Smart, B. P., Ankala, S., Hucke, O., Verlinde, C. L. M. J., Chakrabart, D., Strickland, C., Yokoyama, K., Buckner, F. S., Hamilton, A. D., Williams, D. K., Lombardo, L. J., Floyd, D. & Gelb, H. (2007). Antimicrob. Agents Chemother. 51, 3659-3671.  [PubMed]


Acta Cryst (2012). E68, o3486  [ doi:10.1107/S1600536812048404 ]

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