4WOR
Staphylococcal nuclease in complex with Ca2+ and thymidine-3'-5'-diphosphate (pdTp) at room temperature
Summary for 4WOR
Entry DOI | 10.2210/pdb4wor/pdb |
Related | 1SNC |
Descriptor | Thermonuclease, CALCIUM ION, THYMIDINE-3',5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 1 |
Total formula weight | 17285.60 |
Authors | Wall, M.E.,Ealick, S.E.,Gruner, S.M. (deposition date: 2014-10-16, release date: 2014-10-29, Last modification date: 2023-09-27) |
Primary citation | Wall, M.E.,Ealick, S.E.,Gruner, S.M. Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease. Proc. Natl. Acad. Sci. U.S.A., :6180-6184, 1997 Cited by PubMed Abstract: We have developed methods for obtaining and characterizing three-dimensional maps of the reciprocal-space distribution of diffuse x-ray scattering from protein crystals, and have used the methods to study the nature of disorder in crystals of Staphylococcal nuclease. Experimentally obtained maps are 99.5% complete in the reciprocal-space resolution range of 10 A-2.5 A, show symmetry consistent with the P41 space group of the unit cell, and are highly reproducible. Quantitative comparisons of the data with three-dimensional simulations imply liquid-like motions of the protein [Caspar, D. L. D., Clarage, J., Salunke, D. M. & Clarage, M. (1988) Nature (London) 332, 659-662], with a correlation length of 10 A and a root-mean-square displacement of 0.36 A. PubMed: 9177191DOI: 10.1073/pnas.94.12.6180 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.596 Å) |
Structure validation
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