6HF7
Crystal structure of the adenylate kinase from Methanothermococcus thermolithotrophicus co-crystallized with Tb-Xo4
Summary for 6HF7
| Entry DOI | 10.2210/pdb6hf7/pdb |
| Descriptor | Adenylate kinase, Tb-Xo4, TERBIUM(III) ION, ... (6 entities in total) |
| Functional Keywords | protein crystallization, de novo phasing, nucleation, crystallophore, tb-xo4, molecular glue, lanthanide complex, transferase |
| Biological source | Methanothermococcus thermolithotrophicus (Methanococcus thermolithotrophicus) |
| Total number of polymer chains | 3 |
| Total formula weight | 66123.65 |
| Authors | Engilberge, S.,Wagner, T.,Santoni, G.,Breyton, C.,Shima, S.,Franzetti, B.,Riobe, F.,Maury, O.,Girard, E. (deposition date: 2018-08-21, release date: 2019-06-19, Last modification date: 2024-05-15) |
| Primary citation | Engilberge, S.,Wagner, T.,Santoni, G.,Breyton, C.,Shima, S.,Franzetti, B.,Riobe, F.,Maury, O.,Girard, E. Protein crystal structure determination with the crystallophore, a nucleating and phasing agent. J.Appl.Crystallogr., 52:722-731, 2019 Cited by PubMed Abstract: Obtaining crystals and solving the phase problem remain major hurdles encountered by bio-crystallographers in their race to obtain new high-quality structures. Both issues can be overcome by the crystallophore, Tb-Xo4, a lanthanide-based molecular complex with unique nucleating and phasing properties. This article presents examples of new crystallization conditions induced by the presence of Tb-Xo4. These new crystalline forms bypass crystal defects often encountered by crystallographers, such as low-resolution diffracting samples or crystals with twinning. Thanks to Tb-Xo4's high phasing power, the structure determination process is greatly facilitated and can be extended to serial crystallography approaches. PubMed: 31396026DOI: 10.1107/S1600576719006381 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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