6G89

Thaumatin solved by Native SAD from a dataset collected in 0.6 second with JUNGFRAU detector

Summary for 6G89

• Entry DOI: 10.2210/pdb6g89/pdb
• Descriptor: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: native-sad, jungfrau, integrating detector, plant protein
• Biological source: Thaumatococcus daniellii (Katemfe)
• Total number of polymer chains: 1
• Total formula weight: 22457.14

Authors

Leonarski, F.,Olieric, V.,Vera, L.,Redford, S.,Wang, M. (deposition date: 2018-04-08, release date: 2018-08-01, Last modification date: 2024-10-23)

Primary citation

Leonarski, F.,Redford, S.,Mozzanica, A.,Lopez-Cuenca, C.,Panepucci, E.,Nass, K.,Ozerov, D.,Vera, L.,Olieric, V.,Buntschu, D.,Schneider, R.,Tinti, G.,Froejdh, E.,Diederichs, K.,Bunk, O.,Schmitt, B.,Wang, M.
Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector.
Nat. Methods, 15:799-804, 2018

PubMed Abstract: The accuracy of X-ray diffraction data is directly related to how the X-ray detector records photons. Here we describe the application of a direct-detection charge-integrating pixel-array detector (JUNGFRAU) in macromolecular crystallography (MX). JUNGFRAU features a uniform response on the subpixel level, linear behavior toward high photon rates, and low-noise performance across the whole dynamic range. We demonstrate that these features allow accurate MX data to be recorded at unprecedented speed. We also demonstrate improvements over previous-generation detectors in terms of data quality, using native single-wavelength anomalous diffraction (SAD) phasing, for thaumatin, lysozyme, and aminopeptidase N. Our results suggest that the JUNGFRAU detector will substantially improve the performance of synchrotron MX beamlines and equip them for future synchrotron light sources.

PubMed: 30275593
DOI: 10.1038/s41592-018-0143-7

Experimental method

X-RAY DIFFRACTION (2.359 Å)