Structure of the pig insulin dimer in the cubic crystal.
Atomic coordinates for pig insulin in the cubic crystal have been refined by reciprocal-space methods to an R factor of 0.173 for data between 10.0 and 1.7 A resolution with structure-factor amplitudes greater than two standard deviations. Stereochemical parameters for the refined model are close to standard values and the estimated error in the positions of well-ordered atoms is about 0.1 A. Residues directly involved in the formation of the exact (crystallographic) cubic insulin dimer are oriented similarly to those in the non-crystallographic 2Zn insulin dimer. Other residues, which make different molecular contacts in the different crystal forms, have locally altered conformations. The cubic insulin molecule is significantly more similar to one of the two independent molecules in the 2Zn insulin dimer than the other. This more similar molecule is expected to be the more stable conformer.
Badger
J
J
Department of Physics, University of York, England.
Harris
M R
MR
Reynolds
C D
CD
Evans
A C
AC
Dodson
E J
EJ
Dodson
G G
GG
North
A C
AC
D000818:Animals; D007328:Insulin / Q000737:chemistry*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D013552:Swine; D013816:Thermodynamics; D014961:X-Ray Diffraction / Q000379:methods
D007328:Insulin; D046911:Macromolecular Substances