X-RAY CRYSTALLOGRAPHIC STUDIES OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM P. VERSICOLOR LOBSTER
P.versicolor龙虾D-甘油醛-3-磷酸脱氢酶的X射线晶体学研究——分子置换法结构测定

The P. versicolor lobster tail muscle Holo-D-glyceraldehyde-3-phosphate dehydrogenase has been crystallized. The preliminary crystallographic study shows that GAPDH crystal belongs to C2 space group, there is only half molecule per asymmetric unit and the molecule located at the 2-fold axis. Further X-ray structure analysis at low resolution using molecular replacement technique with the Homarus Americanus lobster GAPDH structure as model structure shows that the subunit arragement within molecule is 222 symmentry, the molecular Q axis is parallel to crystallographic 2-fold axis b and molecular P and R axes are parallel to crystallographic a and c axes respe-ctively. The crystallographic R-factor is 0.46 at 5A resolution. An electrondensity map was calculated at 5A resolution. The structure analyses at higher resolution of several isomophous crystals of this enzyme, especially that with the fluorescent NAD+ derivative, are in progress.