5WR8
Thaumatin structure determined by SACLA at 1.55 Angstrom
Summary for 5WR8
| Entry DOI | 10.2210/pdb5wr8/pdb |
| Descriptor | Thaumatin I, L(+)-TARTARIC ACID (3 entities in total) |
| Functional Keywords | sweet-tasting protein, sweet receptor, plant protein |
| Biological source | Thaumatococcus daniellii (Katemfe) |
| Total number of polymer chains | 1 |
| Total formula weight | 22378.13 |
| Authors | Masuda, T.,Suzuki, M.,Inoue, S.,Sugahara, M. (deposition date: 2016-12-01, release date: 2017-11-29, Last modification date: 2024-10-23) |
| Primary citation | Sugahara, M.,Nakane, T.,Masuda, T.,Suzuki, M.,Inoue, S.,Song, C.,Tanaka, R.,Nakatsu, T.,Mizohata, E.,Yumoto, F.,Tono, K.,Joti, Y.,Kameshima, T.,Hatsui, T.,Yabashi, M.,Nureki, O.,Numata, K.,Nango, E.,Iwata, S. Hydroxyethyl cellulose matrix applied to serial crystallography Sci Rep, 7:703-703, 2017 Cited by PubMed Abstract: Serial femtosecond crystallography (SFX) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3,000 diffraction images. PubMed: 28386083DOI: 10.1038/s41598-017-00761-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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