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Volume 69 
Part 3 
Page m169  
March 2013  

Received 10 February 2013
Accepted 18 February 2013
Online 23 February 2013

Key indicators
Single-crystal X-ray study
T = 293 K
Mean [sigma](C-C) = 0.003 Å
R = 0.033
wR = 0.098
Data-to-parameter ratio = 18.7
Details
Open access

Bis(azido-[kappa]N)bis[4-(dimethylamino)pyridine-[kappa]N]zinc

aUnité de Recherche de Chimie de l'Environnement et Moléculaire Structurale (CHEMS), Faculté des Sciences Exactes, Campus Chaabet Ersas, Université Constantine I, 25000 Constantine, Algeria
Correspondence e-mail: Lamiabendjeddou@yahoo.fr

In the title complex, [Zn(N3)2(C7H10N2)2], the ZnII atom is coordinated by two N atoms from two 4-(dimethylamino)pyridine (DMAP) ligands and by two N atoms from two azide anions in a distorted tetrahedral coordination geometry. In the crystal, weak C-H...N hydrogen bonds between the DMAP and azide ligands link these discrete complex molecules into a three-dimensional supramolecular network.

Related literature

For the property of complexes with a dimethylaminopyridine ligand, see: Araki et al. (2005[Araki, H., Tsuge, K., Sasaki, Y., Ishizaka, S. & Kitamura, N. (2005). Inorg. Chem. 44, 9667-9675.]). For weak hydrogen-bonding modes, 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 related compounds, see: Fu (2000[Fu, G.-C. (2000). Acc. Chem. Res. 33, 412-420.]); Tyrra et al. (2003[Tyrra, W., Naumann, D. & Pantenburg, I. (2003). J. Fluorine Chem. 120, 13-19.]).

[Scheme 1]

Experimental

Crystal data
  • [Zn(N3)2(C7H10N2)2]

  • Mr = 393.79

  • Monoclinic, P 21 /c

  • a = 14.819 (5) Å

  • b = 9.610 (5) Å

  • c = 14.555 (5) Å

  • [beta] = 118.158 (5)°

  • V = 1827.5 (13) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 1.36 mm-1

  • T = 293 K

  • 0.3 × 0.2 × 0.2 mm

Data collection
  • Nonius KappaCCD diffractometer

  • 15768 measured reflections

  • 4302 independent reflections

  • 3323 reflections with I > 2[sigma](I)

  • Rint = 0.019

Refinement
  • R[F2 > 2[sigma](F2)] = 0.033

  • wR(F2) = 0.098

  • S = 1.03

  • 4302 reflections

  • 230 parameters

  • H-atom parameters constrained

  • [Delta][rho]max = 0.31 e Å-3

  • [Delta][rho]min = -0.45 e Å-3

Table 1
Selected bond lengths (Å)

Zn-N1A 2.031 (2)
Zn-N1B 2.018 (2)
Zn-N3 1.935 (3)
Zn-N6 1.969 (3)

Table 2
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
C1A-H1A1...N8i 0.96 2.56 3.484 (4) 163
C5A-H5A...N8ii 0.93 2.59 3.332 (4) 137
C7B-H7B...N3iii 0.93 2.58 3.367 (4) 143
C7B-H7B...N4iii 0.93 2.59 3.382 (4) 143
Symmetry codes: (i) -x+2, -y-1, -z+2; (ii) [-x+2, y-{\script{1\over 2}}, -z+{\script{3\over 2}}]; (iii) -x+1, -y-1, -z+1.

Data collection: KappaCCD Reference Manual (Nonius, 1998[Nonius (1998). KappaCCD Reference Manual. Nonius BV, Delft, The Netherlands.]); cell refinement: DENZO and SCALEPACK (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]); data reduction: DENZO and SCALEPACK[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]; program(s) used to solve structure: SIR2002 (Burla et al., 2003[Burla, M. C., Camalli, M., Carrozzini, B., Cascarano, G. L., Giacovazzo, C., Polidori, G. & Spagna, R. (2003). J. Appl. Cryst. 36, 1103.]); 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, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]); software used to prepare material for publication: WinGX (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]), Mercury (Macrae et al., 2006[Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.]) and POVRay (Persistence of Vision Team, 2004[Persistence of Vision Team (2004). POV-RAY. Persistence of Vision Raytracer Pty Ltd, Victoria, Australia. URL: http://www.povray.org/ .]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: XU5676 ).


Acknowledgements

Technical support (X-ray measurements at SCDRX) by Université Henry Poincaré, Nancy 1, is gratefully acknowledged.

References

Araki, H., Tsuge, K., Sasaki, Y., Ishizaka, S. & Kitamura, N. (2005). Inorg. Chem. 44, 9667-9675.  [ISI] [CSD] [CrossRef] [PubMed] [ChemPort]
Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.  [CrossRef] [ChemPort] [ISI]
Burla, M. C., Camalli, M., Carrozzini, B., Cascarano, G. L., Giacovazzo, C., Polidori, G. & Spagna, R. (2003). J. Appl. Cryst. 36, 1103.  [CrossRef] [details]
Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.  [ISI] [CrossRef] [ChemPort] [details]
Fu, G.-C. (2000). Acc. Chem. Res. 33, 412-420.  [ISI] [CrossRef] [PubMed] [ChemPort]
Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.  [ISI] [CrossRef] [ChemPort] [details]
Nonius (1998). KappaCCD Reference Manual. 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 & R. M. Sweet, pp. 307-326. New York: Academic Press.
Persistence of Vision Team (2004). POV-RAY. Persistence of Vision Raytracer Pty Ltd, Victoria, Australia. URL: http://www.povray.org/ .
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Tyrra, W., Naumann, D. & Pantenburg, I. (2003). J. Fluorine Chem. 120, 13-19.  [ISI] [CSD] [CrossRef] [ChemPort]


Acta Cryst (2013). E69, m169  [ doi:10.1107/S1600536813004686 ]

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