X-ray diffraction images for 5-aminolevulinic acid dehydratase with a putative reaction intermediate resembling the product porphobilinogen bound.

X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase co-crystallised with the substrate 5-aminolevulinic acid. The structure demonstrated a putative product-like intermediate bound covalently to Lys 263 with an amino side chain ligated to the active-site zinc ion in a position normally occupied by a catalytic hydroxide ion. The data were collected in two passes using the ESRF beamline ID29 in Feb 2002 and extend to approximately 1.6 Å resolution.