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6G8B

E. coli Aminopeptidase N solved by Native SAD from a dataset collected in 60 second with JUNGFRAU detector

Summary for 6G8B
Entry DOI10.2210/pdb6g8b/pdb
DescriptorAminopeptidase N, ZINC ION, SODIUM ION, ... (6 entities in total)
Functional Keywordsnative-sad, jungfrau, integrating detector, hydrolase
Biological sourceEscherichia coli (strain K12)
Total number of polymer chains1
Total formula weight102035.10
Authors
Leonarski, F.,Olieric, V.,Redford, S.,Wang, M. (deposition date: 2018-04-08, release date: 2018-08-01, Last modification date: 2024-05-08)
Primary citationLeonarski, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.374 Å)
Structure validation

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