5FGX
Thaumatin solved by native sulphur SAD using synchrotron radiation
Summary for 5FGX
Entry DOI | 10.2210/pdb5fgx/pdb |
Descriptor | Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total) |
Functional Keywords | sulphur sad, synchrotron, plant protein |
Biological source | Thaumatococcus daniellii (Katemfe) |
Cellular location | Cytoplasmic vesicle: P02883 |
Total number of polymer chains | 1 |
Total formula weight | 22377.15 |
Authors | Nass, K.J.,Meinhart, A.,Barends, T.R.M.,Foucar, L.,Gorel, A.,Aquila, A.,Botha, S.,Doak, R.B.,Koglin, J.,Liang, M.,Shoeman, R.L.,Williams, G.J.,Boutet, S.,Schlichting, I. (deposition date: 2015-12-21, release date: 2016-06-08, Last modification date: 2024-11-20) |
Primary citation | Nass, K.,Meinhart, A.,Barends, T.R.,Foucar, L.,Gorel, A.,Aquila, A.,Botha, S.,Doak, R.B.,Koglin, J.,Liang, M.,Shoeman, R.L.,Williams, G.,Boutet, S.,Schlichting, I. Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data. Iucrj, 3:180-191, 2016 Cited by PubMed Abstract: Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms. PubMed: 27158504DOI: 10.1107/S2052252516002980 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.134 Å) |
Structure validation
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