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Volume 69 
Part 4 
Pages o567-o568  
April 2013  

Received 4 March 2013
Accepted 17 March 2013
Online 23 March 2013

Key indicators
Single-crystal X-ray study
T = 100 K
Mean [sigma](C-C) = 0.006 Å
R = 0.060
wR = 0.166
Data-to-parameter ratio = 13.1
Details
Open access

N-Butoxycarbonyl-5-oxo-L-proline ethyl ester

aDepartment of Physics, Thiagarajar College, Madurai 625 009, India, and bX-ray Crystallography Unit, school of Physics, Universiti Sains Malaysia, 11800-USM, Penang, Malaysia
Correspondence e-mail: vasan692000@yahoo.co.in

The molecular structure of the title compound, C12H19NO5, may be visualized as made up of two nearly perpendicular planes [dihedral angle = 87.39 (12)°] and its crystal structure is a good example of C-H...O interactions assuming significance in optimizing supramolecular aggregation in crystals in a molecule which is severely imbalanced in terms of donors to acceptor atoms. The pyrrolidine ring adopts a (3T2) twist conformation with puckering parameters Q = 0.2630 (4) Å and [varphi] = 59 (9)°. The crystal structure features R24(10) and R34(26) ring motifs formed by four weak C-H...O interactions, leading to supramolecular sheets lying parallel to the bc plane.

Related literature

For general background, see: Holladay et al. (1991[Holladay, M. W., Lin, N., May, C. S., Garvey, D. S., Witte, D. G., Miller, T. G., Wolfram, A. W. & Nadzan, A. M. (1991). J. Med. Chem. 34, 455-457.]); Kayushina & Vainshtein (1966[Kayushina, R. L. & Vainshtein, B. K. (1966). Soviet Phys. Crystallogr. 10, 698-706.]); Wu (2009[Wu, G. (2009). Amino Acids, 37, 1-17.]). For the biological activity of proline derivatives, see: Hayashi et al. (2003[Hayashi, S., Tajkhorshid, E. & Schulten, K. (2003). Biophys. J. 85, 1440-1449.]); Nishikawa & Murakami (2005[Nishikawa, T. & Murakami, M. (2005). J. Mol. Biol. 352, 319-328.]). For hydrogen bonding, see: Bernstein et al. (1995[Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N. L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.]). For puckering parameters, see: Cremer & Pople (1975[Cremer, D. & Pople, J. A. (1975). J. Am. Chem. Soc. 97, 1354-1358.]). For a description of the Cambridge Structural Database, see: Allen (2002[Allen, F. H. (2002). Acta Cryst. B58, 380-388.]).

[Scheme 1]

Experimental

Crystal data
  • C12H19NO5

  • Mr = 257.28

  • Orthorhombic, P 21 21 21

  • a = 26.6884 (13) Å

  • b = 5.7650 (3) Å

  • c = 8.7054 (4) Å

  • V = 1339.40 (11) Å3

  • Z = 4

  • Cu K[alpha] radiation

  • [mu] = 0.83 mm-1

  • T = 100 K

  • 0.44 × 0.21 × 0.11 mm

Data collection
  • Bruker SMART APEXII CCD area-detector diffractometer

  • Absorption correction: multi-scan (SADABS; Bruker, 2009[Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.]) Tmin = 0.711, Tmax = 0.914

  • 9641 measured reflections

  • 2184 independent reflections

  • 2144 reflections with I > 2[sigma](I)

  • Rint = 0.049

Refinement
  • R[F2 > 2[sigma](F2)] = 0.060

  • wR(F2) = 0.166

  • S = 1.09

  • 2184 reflections

  • 167 parameters

  • H-atom parameters constrained

  • [Delta][rho]max = 0.37 e Å-3

  • [Delta][rho]min = -0.22 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
C2-H2A...O3i 1.00 2.51 3.436 (5) 154
C3-H3B...O3ii 0.99 2.46 3.095 (5) 121
C6-H6B...O5iii 0.99 2.50 3.344 (5) 143
C12-H12A...O5i 0.98 2.55 3.327 (5) 136
Symmetry codes: (i) x, y-1, z; (ii) [-x+2, y-{\script{1\over 2}}, -z+{\script{1\over 2}}]; (iii) x, y, z+1.

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: SHELXTL (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); program(s) used to refine structure: SHELXTL; molecular graphics: SHELXTL; software used to prepare material for publication: SHELXTL and PLATON (Spek, 2009[Spek, A. L. (2009). Acta Cryst. D65, 148-155.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: BX2436 ).


Acknowledgements

The authors thank Dr MutharasuDevarajan, Associate Professor, and the staff of the X-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, for their help with the data collection.

References

Allen, F. H. (2002). Acta Cryst. B58, 380-388.  [ISI] [CrossRef] [details]
Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N. L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.  [CrossRef] [ChemPort] [ISI]
Bruker (2009). APEX2, SAINT and SADABS. Bruker AXS Inc., Madison, Wisconsin, USA.
Cremer, D. & Pople, J. A. (1975). J. Am. Chem. Soc. 97, 1354-1358.  [CrossRef] [ChemPort] [ISI]
Hayashi, S., Tajkhorshid, E. & Schulten, K. (2003). Biophys. J. 85, 1440-1449.  [ISI] [CrossRef] [PubMed] [ChemPort]
Holladay, M. W., Lin, N., May, C. S., Garvey, D. S., Witte, D. G., Miller, T. G., Wolfram, A. W. & Nadzan, A. M. (1991). J. Med. Chem. 34, 455-457.  [CrossRef] [PubMed] [ChemPort] [ISI]
Kayushina, R. L. & Vainshtein, B. K. (1966). Soviet Phys. Crystallogr. 10, 698-706.
Nishikawa, T. & Murakami, M. (2005). J. Mol. Biol. 352, 319-328.  [ISI] [CrossRef] [PubMed] [ChemPort]
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Spek, A. L. (2009). Acta Cryst. D65, 148-155.  [ISI] [CrossRef] [details]
Wu, G. (2009). Amino Acids, 37, 1-17.  [ISI] [CrossRef] [PubMed]


Acta Cryst (2013). E69, o567-o568   [ doi:10.1107/S1600536813007265 ]

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