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6I5C

Long wavelength native-SAD phasing of Tubulin-Stathmin-TTL complex

Replaces:  4WBN
Summary for 6I5C
Entry DOI10.2210/pdb6i5c/pdb
Related4WBN
DescriptorTubulin alpha-1B chain, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (12 entities in total)
Functional Keywordstubulin complex, t2r-ttl, long-wavelength native-sad phasing, native-sad, s-sad, structural protein
Biological sourceBos taurus (Bovine)
More
Total number of polymer chains6
Total formula weight257658.23
Authors
Primary citationBasu, S.,Olieric, V.,Leonarski, F.,Matsugaki, N.,Kawano, Y.,Takashi, T.,Huang, C.Y.,Yamada, Y.,Vera, L.,Olieric, N.,Basquin, J.,Wojdyla, J.A.,Bunk, O.,Diederichs, K.,Yamamoto, M.,Wang, M.
Long-wavelength native-SAD phasing: opportunities and challenges.
Iucrj, 6:373-386, 2019
Cited by
PubMed Abstract: Native single-wavelength anomalous dispersion (SAD) is an attractive experimental phasing technique as it exploits weak anomalous signals from intrinsic light scatterers ( < 20). The anomalous signal of sulfur in particular, is enhanced at long wavelengths, however the absorption of diffracted X-rays owing to the crystal, the sample support and air affects the recorded intensities. Thereby, the optimal measurable anomalous signals primarily depend on the counterplay of the absorption and the anomalous scattering factor at a given X-ray wavelength. Here, the benefit of using a wavelength of 2.7 over 1.9 Å is demonstrated for native-SAD phasing on a 266 kDa multiprotein-ligand tubulin complex (TR-TTL) and is applied in the structure determination of an 86 kDa helicase Sen1 protein at beamline BL-1A of the KEK Photon Factory, Japan. Furthermore, X-ray absorption at long wavelengths was controlled by shaping a lysozyme crystal into spheres of defined thicknesses using a deep-UV laser, and a systematic comparison between wavelengths of 2.7 and 3.3 Å is reported for native SAD. The potential of laser-shaping technology and other challenges for an optimized native-SAD experiment at wavelengths >3 Å are discussed.
PubMed: 31098019
DOI: 10.1107/S2052252519002756
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.95 Å)
Structure validation

226707

数据于2024-10-30公开中

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