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Volume 68 
Part 11 
Page o3083  
November 2012  

Received 30 September 2012
Accepted 1 October 2012
Online 6 October 2012

Key indicators
Single-crystal X-ray study
T = 298 K
Mean [sigma](C-C) = 0.002 Å
R = 0.043
wR = 0.113
Data-to-parameter ratio = 20.8
Details
Open access

4-Methoxybenzamidinium chloride monohydrate

aChemistry Department, "Sapienza" University of Rome, P.le A. Moro, 5, I-00185 Rome, Italy
Correspondence e-mail: g.portalone@caspur.it

In the cation of the title compound, C8H11N2O+·Cl-·H2O, the C-N bonds of the amidinium group are identical within experiemental error [1.305 (2) and 1.304 (2) Å], and its plane forms a dihedral angle of 25.83 (8)° with the phenyl ring. The ionic components are associated in the crystal into polymeric hydrogen-bonded supramolecular tapes stabilized by N-H+...Cl- and N-H+...Ow intermolecular hydrogen bonds, and by Ow-H...Cl- interactions.

Related literature

For the biological and pharmacological relevance of benzamidine, see: Marquart et al. (1983[Marquart, M., Walter, J., Deisenhofer, J., Bode, W. & Huber, R. (1983). Acta Cryst. B39, 480-490.]); Sprang et al. (1987[Sprang, S., Standing, T., Fletterick, R. J., Strong, R. M., Finer-Moor, J., Xuong, N. H., Hamlin, N. R., Rutter, W. & Kreik, C. S. (1987). Science, 237, 905-909.]); Bode et al. (1990[Bode, W., Turk, D. & Stürzebecher, J. (1990). Eur. J. Biochem. 193, 175-180.]); Powers & Harper (1999[Powers, J. C. & Harper, J. W. (1999). Proteinase inhibitors, edited by A. J. Barrett & G. Salvesen, pp. 55-152. Amsterdam: Elsevier.]); Grzesiak et al. (2000[Grzesiak, A., Helland, R., Smalas, A. O., Krowarsch, D., Dadlez, M. & Otlewski, J. (2000). J. Mol. Biol. 301, 205-217.]). For structural analysis of proton-transfer adducts containing molecules of biological interest, see: Portalone (2011a[Portalone, G. (2011a). Chem. Centr. J. 5, 51.]); Portalone & Irrera (2011[Portalone, G. & Irrera, S. (2011). J. Mol. Struct. 991, 92-96.]). For the supramolecular association in proton-transfer adducts containing benzamidinium cations, see; Portalone (2010[Portalone, G. (2010). Acta Cryst. C66, o295-o301.], 2011b[Portalone, G. (2011b). Acta Cryst. E67, o3394-o3395.], 2012[Portalone, G. (2012). Acta Cryst. E68, o268-o269.]). For hydrogen-bond motifs, see: Bernstein et al. (1995[Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.]).

[Scheme 1]

Experimental

Crystal data
  • C8H11N2O+·Cl-·H2O

  • Mr = 204.65

  • Monoclinic, P 21 /c

  • a = 11.3029 (7) Å

  • b = 9.3142 (5) Å

  • c = 9.9983 (6) Å

  • [beta] = 99.820 (6)°

  • V = 1037.17 (11) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.34 mm-1

  • T = 298 K

  • 0.30 × 0.27 × 0.25 mm

Data collection
  • Oxford Diffraction Xcalibur S CCD diffractometer

  • Absorption correction: multi-scan (CrysAlis RED; Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]) Tmin = 0.905, Tmax = 0.968

  • 7158 measured reflections

  • 2989 independent reflections

  • 1947 reflections with I > 2[sigma](I)

  • Rint = 0.018

Refinement
  • R[F2 > 2[sigma](F2)] = 0.043

  • wR(F2) = 0.113

  • S = 0.97

  • 2989 reflections

  • 144 parameters

  • H atoms treated by a mixture of independent and constrained refinement

  • [Delta][rho]max = 0.22 e Å-3

  • [Delta][rho]min = -0.15 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N1-H1A...Cl1 0.81 (2) 2.85 (2) 3.5523 (18) 145 (2)
N1-H1B...O2W 0.75 (2) 2.06 (2) 2.805 (2) 168 (2)
N2-H2A...Cl1 0.96 (2) 2.25 (2) 3.1850 (16) 164.4 (16)
N2-H2B...Cl1i 0.82 (2) 2.43 (2) 3.201 (2) 157.5 (18)
O2W-HWA...Cl1ii 0.82 (3) 2.36 (3) 3.1731 (18) 170 (3)
O2W-HWB...Cl1iii 0.87 (2) 2.29 (2) 3.1603 (17) 174.8 (19)
Symmetry codes: (i) [-x+1, y-{\script{1\over 2}}, -z+{\script{1\over 2}}]; (ii) -x+1, -y+1, -z+1; (iii) [-x+1, y+{\script{1\over 2}}, -z+{\script{1\over 2}}].

Data collection: CrysAlis CCD (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]); cell refinement: CrysAlis CCD; data reduction: CrysAlis RED (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]); program(s) used to solve structure: SIR97 (Altomare et al., 1999[Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.]); 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, 1997[Farrugia, L. J. (1997). J. Appl. Cryst. 30, 565.]); software used to prepare material for publication: WinGX (Farrugia, 1999[Farrugia, L. J. (1999). J. Appl. Cryst. 32, 837-838.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: QM2085 ).


References

Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.  [ISI] [CrossRef] [ChemPort] [details]
Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.  [CrossRef] [ChemPort] [ISI]
Bode, W., Turk, D. & Stürzebecher, J. (1990). Eur. J. Biochem. 193, 175-180.  [CrossRef] [ChemPort] [PubMed] [ISI]
Farrugia, L. J. (1997). J. Appl. Cryst. 30, 565.  [CrossRef] [details]
Farrugia, L. J. (1999). J. Appl. Cryst. 32, 837-838.  [CrossRef] [ChemPort] [details]
Grzesiak, A., Helland, R., Smalas, A. O., Krowarsch, D., Dadlez, M. & Otlewski, J. (2000). J. Mol. Biol. 301, 205-217.  [ISI] [CrossRef] [PubMed] [ChemPort]
Marquart, M., Walter, J., Deisenhofer, J., Bode, W. & Huber, R. (1983). Acta Cryst. B39, 480-490.  [CrossRef] [ISI] [details]
Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.
Portalone, G. (2010). Acta Cryst. C66, o295-o301.  [CSD] [CrossRef] [details]
Portalone, G. (2011a). Chem. Centr. J. 5, 51.  [CSD] [CrossRef]
Portalone, G. (2011b). Acta Cryst. E67, o3394-o3395.  [CSD] [CrossRef] [details]
Portalone, G. (2012). Acta Cryst. E68, o268-o269.  [CSD] [CrossRef] [details]
Portalone, G. & Irrera, S. (2011). J. Mol. Struct. 991, 92-96.  [ISI] [CSD] [CrossRef] [ChemPort]
Powers, J. C. & Harper, J. W. (1999). Proteinase inhibitors, edited by A. J. Barrett & G. Salvesen, pp. 55-152. Amsterdam: Elsevier.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Sprang, S., Standing, T., Fletterick, R. J., Strong, R. M., Finer-Moor, J., Xuong, N. H., Hamlin, N. R., Rutter, W. & Kreik, C. S. (1987). Science, 237, 905-909.  [CrossRef] [ChemPort] [PubMed] [ISI]


Acta Cryst (2012). E68, o3083  [ doi:10.1107/S1600536812041219 ]

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