PRELIMINARY CRYSTALLOGRAPHIC STUDIES ON THE COENZYME BINDING TO GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM Palinurus versicolor

The three forms of glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor muscle, namelyapo native enzyme, apo calboxymethylated enzyme and the enzyme carrying two fluorescent NAD deriva-tives per tetramer have been crystallized. The space groups and unit cell dimensions of these crystals areisomorphous to each other and to those of three corresponding holo-enzymes saturated with NADreportedin a previous paper suggesting that binding of coenzyme to the apo enzymes does not lead to significantconformational changes involving domain movement as demonstrated in the case of glyceraldehyde-3-phos-phate dehydrogenase from Bacillus stearothermophilus.