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Volume 70 
Part 1 
Page o74  
January 2014  

Received 20 November 2013
Accepted 10 December 2013
Online 18 December 2013

Key indicators
Single-crystal X-ray study
T = 173 K
Mean [sigma](C-C) = 0.003 Å
Disorder in main residue
R = 0.047
wR = 0.125
Data-to-parameter ratio = 11.1
Details
Open access

4,4-Di­fluoro-2,3;5,6-bis­(tetra­methylene)-4-bora-3a,4a-di­aza-s-indacene (LD540)

aDepartment of Chemistry, Nanoscience Center, University of Jyväskylä, PO Box 35, FIN-40014 University of Jyväskylä, Finland
Correspondence e-mail: tanja.m.lahtinen@jyu.fi

The title compound, C18H21BF2N2, is a lipophilic dye based on a BODIPY fluoro­phore backbone, which was developed for microscopic imaging of lipid droplets; the mol­ecule has a planar BODIPY core [dihedral angle between the pyrrole rings = 2.3 (3)°] and two tetra­methyl­ene substituents at the 2,3- and 5,6-positions in a half-chair conformation. One of the tetra­methyl­ene substituents is disordered over two two sets of sites with site occupancies of 0.5. In the crystal, pairs of C-H...F inter­actions link the mol­ecules into inversion dimers. Neighbouring dimers are linked by further C-H...F inter­actions, forming an infinite array. C-H...[pi] and [pi]-[pi] [centroid-centroid distance = 4.360 (3) Å] inter­actions are observed between the BODIPY core and the tetra­methyl­ene substituents of neighbouring dimer pairs.

Related literature

For lipid droplets and fluorescence imaging with LD540, see: Beller et al. (2010[Beller, M., Thiel, K., Thul, P. J. & Jäckle, H. (2010). FEBS Lett. 584, 2176-2182.]); Bickel et al. (2009[Bickel, P. E., Tansey, J. T. & Welte, M. A. (2009). Biochim. Biophys. Acta, 1791, 419-440.]); Spandl et al. (2009[Spandl, J., White, D. J., Peychl, J. & Thiele, C. (2009). Traffic, 10, 1579-1584.]). For related BODIPY structures, see: Uppal et al. (2012[Uppal, T., Hu, C., Fronczek, F. R., Maschek, S., Bobadova-Parvanova, P. & Vicente, M. G. H. (2012). Chem. Eur. J. 18, 3893-3905.]).

[Scheme 1]

Experimental

Crystal data
  • C18H21BF2N2

  • Mr = 314.18

  • Monoclinic, P 21 /n

  • a = 8.8836 (4) Å

  • b = 16.467 (1) Å

  • c = 11.4865 (6) Å

  • [beta] = 111.271 (3)°

  • V = 1565.84 (15) Å3

  • Z = 4

  • Cu K[alpha] radiation

  • [mu] = 0.77 mm-1

  • T = 173 K

  • 0.1 × 0.1 × 0.04 mm

Data collection
  • Nonius KappaCCD diffractometer with APEXII detector

  • Absorption correction: multi-scan (SADABS; Bruker, 2004[Bruker (2004). COLLECT. Bruker AXS Inc., Madison, Wisconsin, USA.]) Tmin = 0.840, Tmax = 1

  • 7413 measured reflections

  • 2511 independent reflections

  • 1902 reflections with I > 2[sigma](I)

  • Rint = 0.054

Refinement
  • R[F2 > 2[sigma](F2)] = 0.047

  • wR(F2) = 0.125

  • S = 1.03

  • 2511 reflections

  • 227 parameters

  • H-atom parameters constrained

  • [Delta][rho]max = 0.17 e Å-3

  • [Delta][rho]min = -0.30 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

Cg1 and Cg2 are the centroids of the N4,C5,C10-C12 and N22,C21,C14-C16 rings, respectively.

D-H...A D-H H...A D...A D-H...A
C23-H23B...F3i 0.96 2.66 3.621 (3) 178
C8-H8B...F2ii 0.97 2.56 3.252 (3) 129
C17-H17A...Cg2iii 0.97 3.10 3.879 (3) 138
Symmetry codes: (i) -x, -y+1, -z; (ii) [x-{\script{1\over 2}}, -y+{\script{1\over 2}}, z-{\script{1\over 2}}]; (iii) -x+1, -y+1, -z+1.

Data collection: COLLECT (Bruker, 2004[Bruker (2004). COLLECT. Bruker AXS Inc., Madison, Wisconsin, USA.]); 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 & R. M. Sweet, pp. 307-326. New York: Academic Press.]); data reduction: DENZO (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter & R. M. Sweet, pp. 307-326. New York: Academic Press.]) and SCALEPACK; 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: OLEX2 (Dolomanov et al., 2009[Dolomanov, O. V., Bourhis, L. J., Gildea, R. J., Howard, J. A. K. & Puschmann, H. (2009). J. Appl. Cryst. 42, 339-341.]); software used to prepare material for publication: OLEX2.


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: VM2201 ).


Acknowledgements

Professor Kari Rissanen is gratefully acknowledged for his help with the data collection and structure refinement. Dr Arto Valkonen and Filip Topic are acknowledged for their help with preparing the CIF file.

References

Beller, M., Thiel, K., Thul, P. J. & Jäckle, H. (2010). FEBS Lett. 584, 2176-2182.  [Web of Science] [CrossRef] [ChemPort] [PubMed]
Bickel, P. E., Tansey, J. T. & Welte, M. A. (2009). Biochim. Biophys. Acta, 1791, 419-440.  [Web of Science] [CrossRef] [PubMed] [ChemPort]
Bruker (2004). COLLECT. Bruker AXS Inc., Madison, Wisconsin, USA.
Dolomanov, O. V., Bourhis, L. J., Gildea, R. J., Howard, J. A. K. & Puschmann, H. (2009). J. Appl. Cryst. 42, 339-341.  [Web of Science] [CrossRef] [ChemPort] [IUCr Journals]
Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter & R. M. Sweet, pp. 307-326. New York: Academic Press.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [ChemPort] [IUCr Journals]
Spandl, J., White, D. J., Peychl, J. & Thiele, C. (2009). Traffic, 10, 1579-1584.  [CrossRef] [PubMed] [ChemPort]
Uppal, T., Hu, C., Fronczek, F. R., Maschek, S., Bobadova-Parvanova, P. & Vicente, M. G. H. (2012). Chem. Eur. J. 18, 3893-3905.  [CSD] [CrossRef] [ChemPort] [PubMed]


Acta Cryst (2014). E70, o74  [ doi:10.1107/S1600536813033448 ]

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