6A44
R1EN(5-227)-ubiquitin fusion
Summary for 6A44
| Entry DOI | 10.2210/pdb6a44/pdb |
| Related | 1UBQ 2EI9 |
| Descriptor | RNA-directed DNA polymerase homolog (R1),Polyubiquitin-C, ACETIC ACID (3 entities in total) |
| Functional Keywords | endonuclease, chimera, dna binding protein |
| Biological source | Bombyx mori (Silk moth) More |
| Total number of polymer chains | 1 |
| Total formula weight | 33598.21 |
| Authors | Maita, N. (deposition date: 2018-06-19, release date: 2018-10-24, Last modification date: 2024-11-13) |
| Primary citation | Maita, N. Crystal Structure Determination of Ubiquitin by Fusion to a Protein That Forms a Highly Porous Crystal Lattice J. Am. Chem. Soc., 140:13546-13549, 2018 Cited by PubMed Abstract: The protein crystallization process requires screening of a large number of conditions using a large quantity of high-purity protein, which makes crystal structure analysis difficult. Thus, the development of easy and versatile protein crystallization techniques is both extremely desirable and highly challenging. Here I demonstrate the crystallization and structure determination of ubiquitin by genetic fusion to the highly porous honeycomb lattice of R1EN. I successfully crystallized and collected X-ray data from three R1EN-ubiquitin constructs with various linker lengths under the same conditions as the original R1EN. The crystals diffracted to 1.7-2.4 Å resolution, and the ubiquitin structures were determined with results almost identical to the previously published structure. Moreover, the ubiquitin structure could be solved by molecular replacement using R1EN alone. This method may reduce the effort required for crystallization screening and is applicable to de novo protein structure determination. PubMed: 30299944DOI: 10.1021/jacs.8b07512 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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