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Volume 66 
Part 6 
Page o1330  
June 2010  

Received 23 April 2010
Accepted 6 May 2010
Online 12 May 2010

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Key indicators
Single-crystal X-ray study
T = 150 K
Mean [sigma](C-C) = 0.004 Å
R = 0.040
wR = 0.095
Data-to-parameter ratio = 8.7
Details
Open access

1-Deoxy-1-fluoro-L-galactitol

Sarah F. Jenkinson,a* Daniel Best,a Ken Izumori,b Francis X. Wilson,c Alexander C. Weymouth-Wilson,d George W. J. Fleeta and Amber L. Thompsone

aDepartment of Organic Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3TA, England,bRare Sugar Research Centre, Kagawa University, 2393 Miki-cho, Kita-gun, Kagawa 761-0795, Japan,cSummit PLC, 91 Milton Park, Abingdon, Oxon, OX14 4RY, England,dDextra Laboratories Ltd, Science and Technology Centre, Whiteknights Road, Reading RG6 6BZ, England, and eDepartment of Chemical Crystallography, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3TA, England
Correspondence e-mail: sarah.jenkinson@chem.ox.ac.uk

The crystal structure unequivocally confirms the relative stereochemistry of the title compound, C6H13FO5 [6-deoxy-6-fluoro-D-galactitol or (2S,3R,4R,5S)-6-fluorohexane-1,2,3,4,5-pentaol]. The absolute stereochemistry was determined from the use of D-galactose as the starting material. In the crystal, the molecules are linked by O-H...O and O-H...F hydrogen bonds, forming a three-dimensional network with each molecule acting as a donor and acceptor for five hydrogen bonds.

Related literature

For literature regarding fluorogalactitol and fluorogalactose, see: Kent & Wright (1972[Kent, P. W. & Wright, J. R. (1972). Carbohydr. Res. 22, 193-200.]); Jenkinson et al. (2010[Jenkinson, S. F., Best, D., Izumori, K., Wilson, F. X., Weymouth-Wilson, A. C., Fleet, G. W. J. & Thompson, A. L. (2010). Acta Cryst. E66, o1315.]).

[Scheme 1]

Experimental

Crystal data

  • C6H13FO5

  • Mr = 184.16

  • Monoclinic, P 21

  • a = 4.7968 (3) Å

  • b = 8.5957 (5) Å

  • c = 9.8194 (7) Å

  • [beta] = 103.233 (3)°

  • V = 394.12 (4) Å3

  • Z = 2

  • Mo K[alpha] radiation

  • [mu] = 0.15 mm-1

  • T = 150 K

  • 0.40 × 0.10 × 0.05 mm
Data collection

  • Area diffractometer

  • Absorption correction: multi-scan (DENZO/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.]) Tmin = 0.88, Tmax = 0.99

  • 3069 measured reflections

  • 947 independent reflections

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

  • Rint = 0.039
Refinement

  • R[F2 > 2[sigma](F2)] = 0.040

  • wR(F2) = 0.095

  • S = 0.99

  • 947 reflections

  • 109 parameters

  • 1 restraint

  • H-atom parameters constrained

  • [Delta][rho]max = 0.35 e Å-3

  • [Delta][rho]min = -0.36 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
O4-H41...O8i 0.82 1.94 2.738 (4) 165
O10-H101...O12ii 0.82 1.95 2.730 (4) 160
O8-H81...O10iii 0.82 1.87 2.691 (4) 172
O6-H61...O4iv 0.82 1.89 2.703 (4) 170
O12-H121...F1v 0.84 2.08 2.895 (3) 163
Symmetry codes: (i) [-x+2, y-{\script{1\over 2}}, -z+1]; (ii) [-x+1, y+{\script{1\over 2}}, -z]; (iii) x+1, y, z; (iv) x-1, y, z; (v) x-1, y, z-1.

Data collection: COLLECT (Nonius, 2001[Nonius (2001). COLLECT. Nonius BV, Delft, The Netherlands.]); cell refinement: DENZO/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/SCALEPACK; program(s) used to solve structure: SIR92 (Altomare et al., 1994[Altomare, A., Cascarano, G., Giacovazzo, C., Guagliardi, A., Burla, M. C., Polidori, G. & Camalli, M. (1994). J. Appl. Cryst. 27, 435.]); program(s) used to refine structure: CRYSTALS (Betteridge et al., 2003[Betteridge, P. W., Carruthers, J. R., Cooper, R. I., Prout, K. & Watkin, D. J. (2003). J. Appl. Cryst. 36, 1487.]); molecular graphics: CAMERON (Watkin et al., 1996[Watkin, D. J., Prout, C. K. & Pearce, L. J. (1996). CAMERON. Chemical Crystallography Laboratory, Oxford, England.]); software used to prepare material for publication: CRYSTALS.

Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: LH5036 ).

References

Altomare, A., Cascarano, G., Giacovazzo, C., Guagliardi, A., Burla, M. C., Polidori, G. & Camalli, M. (1994). J. Appl. Cryst. 27, 435.  [CrossRef] [details]
Betteridge, P. W., Carruthers, J. R., Cooper, R. I., Prout, K. & Watkin, D. J. (2003). J. Appl. Cryst. 36, 1487.  [CrossRef] [details]
Jenkinson, S. F., Best, D., Izumori, K., Wilson, F. X., Weymouth-Wilson, A. C., Fleet, G. W. J. & Thompson, A. L. (2010). Acta Cryst. E66, o1315.  [CrossRef] [details]
Kent, P. W. & Wright, J. R. (1972). Carbohydr. Res. 22, 193-200.  [CrossRef] [ChemPort] [PubMed] [ISI]
Nonius (2001). COLLECT. 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.
Watkin, D. J., Prout, C. K. & Pearce, L. J. (1996). CAMERON. Chemical Crystallography Laboratory, Oxford, England.

Acta Cryst (2010). E66, o1330  [ doi:10.1107/S1600536810016624 ]

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