1C0C
BOVINE PANCREATIC RIBONUCLEASE A DESICCATED FOR 4.0 DAYS
Summary for 1C0C
Entry DOI | 10.2210/pdb1c0c/pdb |
Related | 1BEL |
Descriptor | RIBONUCLEASE A, SULFATE ION (3 entities in total) |
Functional Keywords | hydrolase (phosphoric diester, rna), desiccated, dry, dehydrated, hydrolase |
Biological source | Bos taurus (cattle) |
Cellular location | Secreted: P61823 |
Total number of polymer chains | 1 |
Total formula weight | 14350.92 |
Authors | Bell, J.A. (deposition date: 1999-07-15, release date: 1999-10-14, Last modification date: 2024-10-30) |
Primary citation | Bell, J.A. X-ray crystal structures of a severely desiccated protein Protein Sci., 8:2033-2040, 1999 Cited by PubMed Abstract: Unlike most protein crystals, form IX of bovine pancreatic ribonuclease A diffracts well when severely dehydrated. Crystal structures have been solved after 2.5 and 4 days of desiccation with CaSO4, at 1.9 and 2.0 A resolution, respectively. The two desiccated structures are very similar. An RMS displacement of 1.6 A is observed for main-chain atoms in each structure when compared to the hydrated crystal structure with some large rearrangements observed in loop regions. The structural changes are the result of intermolecular contacts formed by strong electrostatic interactions in the absence of a high dielectric medium. The electron density is very diffuse for some surface loops, consistent with a very disordered structure. This disorder is related to the conformational changes. These results help explain conformational changes during the lyophilization of protein and the associated phenomena of denaturation and molecular memory. PubMed: 10548049PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
