The crystal structure of deshexapeptide(B25-B30)insulin at 0.25 nm resolution

The determination of deshexapeptide(B25-B30)insulin(DHI)was divided into two steps.At the first step,the rough structure model of DHI molecule was determined by using the molecularreplacement method associated with the molecular close-packing method at 0.30 nm resolution based on the re-flection data collected on four-cycle diffractometer.At the second step,the DHI model was adjusted and re-fined at 0.25nm resolution based on the data collected on Area Detector.40 water molecules were determinedduring the refinement,the final R-factor is 0.185 with R.M.S.deviation of 0.002nm for bond lengths and 1.9°for bond angles.The differences in conformation and function of DHI with other insulin analogues werecompared and discussed.