8FZU
The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Thr-Val linker variant, Expressed with SUMO tag
Summary for 8FZU
| Entry DOI | 10.2210/pdb8fzu/pdb |
| Related | 8E1F 8FZ3 8FZ4 8FZ6 8FZ8 |
| Descriptor | Transcription factor ETV6,Anthrax toxin receptor 2, POTASSIUM ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | telsam fusion, polymer forming crystallization chaperone, peptide binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 86252.46 |
| Authors | Gajjar, P.L.,Litchfield, C.M.,Callahan, M.,Redd, N.,Doukov, T.,Lebedev, A.,Moody, J.D. (deposition date: 2023-01-30, release date: 2023-07-19, Last modification date: 2023-10-18) |
| Primary citation | Gajjar, P.L.,Pedroza Romo, M.J.,Litchfield, C.M.,Callahan, M.,Redd, N.,Nawarathnage, S.,Soleimani, S.,Averett, J.,Wilson, E.,Lewis, A.,Stewart, C.,Tseng, Y.J.,Doukov, T.,Lebedev, A.,Moody, J.D. Increasing the bulk of the 1TEL-target linker and retaining the 10×His tag in a 1TEL-CMG2-vWa construct improves crystal order and diffraction limits. Acta Crystallogr D Struct Biol, 79:925-943, 2023 Cited by PubMed Abstract: TELSAM-fusion crystallization has the potential to become a revolutionary tool for the facile crystallization of proteins. TELSAM fusion can increase the crystallization rate and enable crystallization at low protein concentrations, in some cases with minimal crystal contacts [Nawarathnage et al. (2022), Open Biol. 12, 210271]. Here, requirements for the linker composition between 1TEL and a fused CMG2 vWa domain were investigated. Ala-Ala, Ala-Val, Thr-Val and Thr-Thr linkers were evaluated, comparing metrics for crystallization propensity and crystal order. The effect on crystallization of removing or retaining the purification tag was then tested. It was discovered that increasing the linker bulk and retaining the 10×His purification tag improved the diffraction resolution, likely by decreasing the number of possible vWa-domain orientations in the crystal. Additionally, it was discovered that some vWa-domain binding modes are correlated with scrambling of the 1TEL polymer orientation in crystals and an effective mitigation strategy for this pathology is presented. PubMed: 37747038DOI: 10.1107/S2059798323007246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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