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Volume 68 
Part 11 
Page o3111  
November 2012  

Received 13 August 2012
Accepted 26 September 2012
Online 13 October 2012

Key indicators
Single-crystal X-ray study
T = 90 K
Mean [sigma](C-C) = 0.002 Å
Disorder in main residue
R = 0.039
wR = 0.102
Data-to-parameter ratio = 14.7
Details
Open access

rac-(Z)-Methyl 1-benzyl-3-[(3-hydroxyquinuclidin-2-ylidene)methyl]-1H-indole-6-carboxylate

aDept. of Pharm. Sciences, College of Pharmacy, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA, and bDept. of Chemistry, University of Kentucky, Lexington KY 40506, USA
Correspondence e-mail: pacrooks@uams.edu

In the title compound, C25H26N2O3, the double bond connecting the aza-bicyclic and indole units has Z geometry. The compound was obtained as a racemate, and since the crystal is centrosymmetric it contains equal amounts of the S and R enantiomers. However, the structure is disordered such that the asymmetric unit contains both enantiomers in unequal amounts [refined occupancies 0.904 (2) and 0.096 (2)]. The dihedral angle between the benzene ring of the benzyl group and the mean plane of the indole ring is 76.07 (3) °. In the crystal, molecules are linked by O-H...Ocarbonyl hydrogen bonds into chains propagating in [110].

Related literature

For background literature, see: Sekhar et al., (2003[Sekhar, K. R., Crooks, P. A., Sonar, V. N., Friedman, D. B., Chan, J. Y., Meredith, M. J., Stames, J. H., Kelton, K. R., Summar, S. R., Sasi, S. & Freeman, M. L. (2003). Cancer Res. 63, 5636-5645.]), Amudhan et al., (2010[Amudhan, V., Reddy, Y. T., Sonar, V. N., Venkatraj, M., Crooks, P. A., Michael, L., Freeman, M. L. & Sekhar, K. R. (2010). Bioorg. Med. Chem. Lett. 20, 7323-7326.]). For the biological activity of N-benzyl indole quinuclidinone, see: Sonar et al. (2007[Sonar, V. N., Reddy, Y. T., Sekhar, K. R., Sowmya, S., Freeman, M. L. & Crooks, P. A. (2007). Bioorg. Med. Chem. Lett. 17(24), 6821-6824.]). For a similar crystal structure, see: Sonar et al., (2004[Sonar, V. N., Parkin, S. & Crooks, P. A. (2004). Acta Cryst. C60, o659-o661.]).

[Scheme 1]

Experimental

Crystal data
  • C25H26N2O3

  • Mr = 402.48

  • Triclinic, [P \overline 1]

  • a = 6.1619 (1) Å

  • b = 10.3119 (2) Å

  • c = 16.5959 (3) Å

  • [alpha] = 75.6705 (7)°

  • [beta] = 80.0939 (7)°

  • [gamma] = 85.9410 (7)°

  • V = 1006.04 (3) Å3

  • Z = 2

  • Mo K[alpha] radiation

  • [mu] = 0.09 mm-1

  • T = 90 K

  • 0.28 × 0.22 × 0.12 mm

Data collection
  • Nonius KappaCCD diffractometer

  • 9126 measured reflections

  • 4597 independent reflections

  • 3831 reflections with I > 2[sigma](I)

  • Rint = 0.024

Refinement
  • R[F2 > 2[sigma](F2)] = 0.039

  • wR(F2) = 0.102

  • S = 1.04

  • 4597 reflections

  • 312 parameters

  • 64 restraints

  • H-atom parameters constrained

  • [Delta][rho]max = 0.27 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
O1-H1A...O2i 0.84 1.97 2.7989 (13) 169
Symmetry code: (i) x-1, y-1, z.

Data collection: COLLECT (Nonius, 1998[Nonius (1998). COLLECT. Nonius, BV, Delft, The Netherlands.]); cell refinement: SCALEPACK (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr and R. M. Sweet, pp. 307-326. New York: Academic Press.]); data reduction: DENZO-SMN (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr and R. M. Sweet, pp. 307-326. New York: Academic Press.]); 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: XP in SHELXTL (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); software used to prepare material for publication: SHELXL97 and local procedures.


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: HG5242 ).


Acknowledgements

This investigation was supported by NIH/National Cancer Institute grant PO1 CA140409.

References

Amudhan, V., Reddy, Y. T., Sonar, V. N., Venkatraj, M., Crooks, P. A., Michael, L., Freeman, M. L. & Sekhar, K. R. (2010). Bioorg. Med. Chem. Lett. 20, 7323-7326.  [PubMed]
Nonius (1998). COLLECT. Nonius, BV, Delft, The Netherlands.
Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr and R. M. Sweet, pp. 307-326. New York: Academic Press.
Sekhar, K. R., Crooks, P. A., Sonar, V. N., Friedman, D. B., Chan, J. Y., Meredith, M. J., Stames, J. H., Kelton, K. R., Summar, S. R., Sasi, S. & Freeman, M. L. (2003). Cancer Res. 63, 5636-5645.  [ISI] [PubMed] [ChemPort]
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Sonar, V. N., Parkin, S. & Crooks, P. A. (2004). Acta Cryst. C60, o659-o661.  [CSD] [CrossRef] [details]
Sonar, V. N., Reddy, Y. T., Sekhar, K. R., Sowmya, S., Freeman, M. L. & Crooks, P. A. (2007). Bioorg. Med. Chem. Lett. 17(24), 6821-6824.  [CrossRef]


Acta Cryst (2012). E68, o3111  [ doi:10.1107/S1600536812040731 ]

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