Racemic crystallography

Racemic crystal structure of Rv1738 from Mycobacterium tuberculosis produced by racemic protein crystallography

Racemic crystallography is a technique used in structural biology where crystals of a protein molecule are developed from an equimolar mixture of an L-protein molecule of natural chirality and its D-protein mirror image.[1][2] L-protein molecules consist of 'left-handed' L-amino acids and the achiral amino acid glycine, whereas the mirror image D-protein molecules consist of 'right-handed' D-amino acids and glycine. Typically, both the L-protein and the D-protein are prepared by total chemical synthesis.

  1. ^ Yeates TO, Kent SB (2012-06-09). "Racemic protein crystallography". Annual Review of Biophysics. 41 (1): 41–61. doi:10.1146/annurev-biophys-050511-102333. PMID 22443988.
  2. ^ Matthews BW (June 2009). "Racemic crystallography--easy crystals and easy structures: what's not to like?". Protein Science. 18 (6): 1135–1138. doi:10.1002/pro.125. PMC 2774423. PMID 19472321.