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Crystal structural studies of destripeptide (B28-B30) insulin
Single crystals of destripeptide (B28-B30) insulin (DTRI) in three forms were obtained by hanging-drop vapor diffusion method. Form 1 belongs to P21 space group with cell parametersa=4.77 nmb=6.19 nmc=6.12nm β=110.3°. Form 2 belongs to P4122 or P4322 space group with cell parametersa= 6.45 nm,c=12.0...
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Published in: | Science China. Chemistry 2000-04, Vol.43 (2), p.178-186 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Single crystals of destripeptide (B28-B30) insulin (DTRI) in three forms were obtained by hanging-drop vapor diffusion method. Form 1 belongs to P21 space group with cell parametersa=4.77 nmb=6.19 nmc=6.12nm β=110.3°. Form 2 belongs to P4122 or P4322 space group with cell parametersa= 6.45 nm,c=12.07 nm. Form 3 belongs to P212121 space group with cell parametersa=4.98 nmb=5.16 nmc=10.06 nm. The structure of form 1 crystal was determined by molecular replacement method and refined at 0.23 nm resolution. The R-factor of the final model is 18.8% with r.m.s. deviations of 0.001 5 nm and 3.3° for the bond lengths and the bond angles, respectively. Studies on the crystal structure show that the removal of B28 Pro has brought DTRI structural changes which made it dissociate more easily than native insulin although DTRI can still form a hexamer. |
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ISSN: | 1006-9291 1674-7291 1862-2771 1869-1870 |
DOI: | 10.1007/BF03027308 |