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5FGX

Thaumatin solved by native sulphur SAD using synchrotron radiation

Summary for 5FGX
Entry DOI10.2210/pdb5fgx/pdb
DescriptorThaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
Functional Keywordssulphur sad, synchrotron, plant protein
Biological sourceThaumatococcus daniellii (Katemfe)
Cellular locationCytoplasmic vesicle: P02883
Total number of polymer chains1
Total formula weight22377.15
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 citationNass, 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: 27158504
DOI: 10.1107/S2052252516002980
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.134 Å)
Structure validation

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数据于2025-07-30公开中

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