A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarking

Trewhella, J.; Vachette, P.; Bierma, J.; Blanchet, C.; Brookes, E.; Chakravarthy, S.; Chatzimagas, L.; Cleveland, T.E.; Cowieson, N.; Crossett, B.; Duff, A.P.; Franke, D.; Gabel, F.; Gillilan, R.E.; Graewert, M.; Grishaev, A.; Guss, J.M.; Hammel, M.; Hopkins, J.; Huang, Q.; Hub, J.S.; Hura, G.L.; Irving, T.C.; Jeffries, C.M.; Jeong, C.; Kirby, N.; Krueger, S.; Martel, A.; Matsui, T.; Li, N.; Pérez, J.; Porcar, L.; Prangé, T.; Rajkovic, I.; Rocco, M.; Rosenberg, D.J.; Ryan, T.M.; Seifert, S.; Sekiguchi, H.; Svergun, D.; Teixeira, S.; Thureau, A.; Weiss, T.M.; Whitten, A.E.; Wood, K.; Zuo, X.

doi:10.1107/S2059798322009184

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 2
Distribution of Guinier and P(r)-derived R_g values, d_max values and the Porod volume to molecular mass ratio (V_P/m) for the data contributing to the consensus SAXS profiles for each protein. Individual experimental values are represented as black open squares, with horizontal offsets for clarity and error bars for R_g values (standard errors). Red squares represent the mean values for each set, with error bars indicating ±1 standard deviation.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 11| November 2022| Pages 1315-1336

https://doi.org/10.1107/S2059798322009184

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