Redetermined structure of β-dl-me­thio­nine at 105 K: an example of the importance of freely refining the positions of the amino-group H atoms

Görbitz, C.H.

doi:10.1107/S1600536814022223

Acta Crystallographica Section E
Acta Crystallographica
Section E CRYSTALLOGRAPHIC COMMUNICATIONS

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Figure 1
(a) The structure of DL-methionine, (I)

, viewed approximately along the N1—C2 bond vector, with 50% probability thermal displacement ellipsoids. The racemate contains molecules of both hands; the one depicted here is the D-enantiomer. Carboxylate groups of three neighboring amino acids accepting hydrogen bonds are shown in a lighter tone. O2ⁱ is at (−x, y + $[{1\over 2}]$ , −z + $[{1\over 2}]$ ), O2ⁱⁱ at (x + $[{1\over 2}]$ , −y, z) and Oⁱⁱⁱ at (x + $[{1\over 2}]$ , −y + 1, z), see Table 2

. Compared to the previously published structure shown in capped sticks representation in (b) (Alagar et al., 2005

), the amino group has been rotated clockwise by about 13.5° to give shorter and more linear hydrogen bonds.

CRYSTALLOGRAPHIC
COMMUNICATIONS

ISSN: 2056-9890

Volume 70| Part 11| October 2014| Pages 341-343

doi:10.1107/S1600536814022223

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