9FCR
Crystal structure of RBBP9 with spacegroup p212121
Summary for 9FCR
| Entry DOI | 10.2210/pdb9fcr/pdb |
| Descriptor | Serine hydrolase RBBP9 (2 entities in total) |
| Functional Keywords | regulation of cell proliferation and differentiation, cell cycle |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 42051.80 |
| Authors | Gorrec, F.,Bellini, D. (deposition date: 2024-05-15, release date: 2024-09-11, Last modification date: 2025-04-16) |
| Primary citation | Caspy, I.,Tang, S.,Bellini, D.,Gorrec, F. A generic cross-seeding approach to protein crystallization. J.Appl.Crystallogr., 58:383-391, 2025 Cited by PubMed Abstract: Obtaining diffraction-quality crystals is often the rate-limiting step during structure determination of biological macromolecules by X-ray crystallography. To address this problem, we investigated a cross-seeding approach with a mixture integrating a heterogeneous set of protein crystal fragments to be used as generic seeds. The fragments are nanometre-sized templates chosen to promote crystal nucleation of protein samples unrelated to the proteins forming the seeds. An atypical crystal form of the human serine hydrolase retinoblastoma binding protein 9 was obtained by adding the mixture to the protein sample before performing standard crystallization assays. The structure was solved by X-ray crystallography at 1.4 Å resolution. Follow-up experiments showed that crystal fragments of α-amylase were critical components in this particular result. The limitations and future applications of our experimental developments are discussed. PubMed: 40170961DOI: 10.1107/S1600576725000457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.37 Å) |
Structure validation
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