Received 8 March 2013
aInstitute for Research in Molecular Medicine, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia,bFaculty of Pharmaceutical Science, UCSI (University College Sedaya International) University, Kuala Lumpur, Malaysia, and cX-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia
Correspondence e-mail: firstname.lastname@example.org
The asymmetric unit of the title compound, C29H24FNO5·0.5CH3OH, contains two independent molecules and a one methanol solvent molecule. The methanol molecule is O-HO hydrogen bonded to one of the independent molecules. The pyrrolidine rings in both molecules adopt half-chair conformations, while the cyclopentane rings within the indane groups are in flattened envelope conformations, with the spiro C atoms forming the flaps. The benzene rings of the indane ring systems form a dihedral angle of 35.06 (7)° in one independent molecule and 31.16 (8)° in the other. The fluoro-substituted benzene ring forms dihedral angles of 65.35 (6) and 85.87 (7)° with the indane group benzene rings in one molecule, and 72.78 (8) and 77.27 (8)° in the other. In each molecule, a weak intramolecular C-HO hydrogen bond forms an S(6) ring motif. In the crystal, weak C-HO, C-HN and C-HF hydrogen bonds link the molecules into a three-dimensional network.
For background to compounds with antitubercular activity, see: Ali et al. (2011). For related structures, see: Wei et al. (2011, 2012). For hydrogen-bond motifs, see: Bernstein et al. (1995). For ring conformations, see: Cremer & Pople (1975). For the stability of the temperature controller used in the data collection, see: Cosier & Glazer (1986).
Data collection: APEX2 (Bruker, 2009); cell refinement: SAINT (Bruker, 2009); data reduction: SAINT; program(s) used to solve structure: SHELXTL (Sheldrick, 2008); program(s) used to refine structure: SHELXTL; molecular graphics: SHELXTL; software used to prepare material for publication: SHELXTL and PLATON (Spek, 2009).
Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: LH5596 ).
The authors wish to express their gratitude and appreciation to the Pharmacogenetics and Novel Therapeutics Research Cluster, Institute for Research in Molecular Medicine, Universiti Sains Malaysia (USM), Penang, for support of this work. This work was funded through Research Grant No. RUC (1001/PSK/8620012) and HiCoE Research Grant No (311.CIPPM.4401005). IAR also thanks USM for the Short Term Grant, No. 304/PFIZIK/6312078.
Ali, M. A., Ismail, R., Choon, T. S., Pandian, S. & Ansari, M. Z. H. (2011). J. Enzyme Inhib. Med. Chem. 26, 598-602.
Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.
Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.
Cosier, J. & Glazer, A. M. (1986). J. Appl. Cryst. 19, 105-107.
Cremer, D. & Pople, J. A. (1975). J. Am. Chem. Soc. 97, 1354-1358.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
Spek, A. L. (2009). Acta Cryst. D65, 148-155.
Wei, A. C., Ali, M. A., Choon, T. S., Arshad, S. & Razak, I. A. (2012). Acta Cryst. E68, o1265-o1266.
Wei, A. C., Ali, M. A., Yoon, Y. K., Quah, C. K. & Fun, H.-K. (2011). Acta Cryst. E67, o3274.