5ANE
Crystal structure of CDK2 in complex with 6-methoxy-7H-purine processed with the CrystalDirect automated mounting and cryo-cooling technology
Summary for 5ANE
| Entry DOI | 10.2210/pdb5ane/pdb |
| Related | 5AMW 5AMX 5AMY 5AMZ 5AN2 5AN4 5AND 5ANG 5ANI 5ANJ 5ANK 5ANL 5ANO |
| Descriptor | CYCLIN-DEPENDENT KINASE 2, 6-METHOXY-9H-PURINE (3 entities in total) |
| Functional Keywords | transferase, protein kinase, inhibitor, automated crystal harvesting, automated cryo-cooling, crystaldirect |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 34126.63 |
| Authors | Zander, U.,Hoffmann, G.,Mathieu, M.,Marquette, J.-P.,Cornaciu, I.,Cipriani, F.,Marquez, J.A. (deposition date: 2015-09-07, release date: 2016-04-13, Last modification date: 2024-05-08) |
| Primary citation | Zander, U.,Hoffmann, G.,Cornaciu, I.,Marquette, J.-P.,Papp, G.,Landret, C.,Seroul, G.,Sinoir, J.,Roewer, M.,Felisaz, F.,Rodriguez-Puente, S.,Mariaule, V.,Murphy, P.,Mathieu, M.,Cipriani, F.,Marquez, J.A. Automated Harvesting and Processing of Protein Crystals Through Laser Photoablation. Acta Crystallogr.,Sect.D, 72:454-, 2016 Cited by PubMed Abstract: Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities. PubMed: 27050125DOI: 10.1107/S2059798316000954 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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