CRYSTAL-STRUCTURE OF DESHEXAPEPTIDE (B25-30) INSULIN AT 0.15 NM RESOLUTION

Citation
Jj. Yue et al., CRYSTAL-STRUCTURE OF DESHEXAPEPTIDE (B25-30) INSULIN AT 0.15 NM RESOLUTION, Progress in Natural Science, 8(1), 1998, pp. 106-112
Citations number
18
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
10020071
Volume
8
Issue
1
Year of publication
1998
Pages
106 - 112
Database
ISI
SICI code
1002-0071(1998)8:1<106:COD(IA>2.0.ZU;2-W
Abstract
The crystal structure of deshexapeptide (B25-30) insulin has been refi ned to a resolution of 0.15 nm, using atomic coordinates of DH I struc ture determined at 0.25 nm resolution, through the use of the differen ce Fourier method and restrained least-squares method interspersed wit h careful review of the electron density map. After refinement, 54 wat er molecules with different occupancy factors were included in the fin al model!. The final crystallographic reliability R-factor is 0.187 in the 1.0-0.15 nm range of resolution. The root-mean-square deviations from the ideal bond lengths and bond angles are 0.001 6 nm and 2.7 deg rees respectively. The conformation and function of DH I and other ins ulin analogues have been discussed.