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 molecular replacement method associated with the molecular close-packing method at 0.30 nm resolution based on the reflection data collected on four-cycle diffractometer. At the second step, the DHI model was adjusted and refined at 0.25 nm resolution based on the data collected on Area Detector. 40 water molecules were determined during the refinement, the final R-factor is 0.185 with R.M.S. deviation of 0.002 nm for bond lengths and 1.9 degrees for bond angles. The differences in conformation and function of DHI with other insulin analogues were compared and discussed.
Chang
W
W
State key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Jiang
T
T
Ren
Z
Z
Wan
Z
Z
Xu
Y
Y
Liang
D
D
Zhu
S
S
Zhang
Y
Y
D007328:Insulin / Q000031:analogs & derivatives* / Q000737:chemistry; D008968:Molecular Conformation
D007328:Insulin; C038071:insulin, deshexapeptide(B25-B30)-