PT  - JOURNAL ARTICLE
AU  - Richard J. Gildea
AU  - James Beilsten-Edmands
AU  - Danny Axford
AU  - Sam Horrell
AU  - Pierre Aller
AU  - James Sandy
AU  - Juan Sanchez-Weatherby
AU  - C. David Owen
AU  - Petra Lukacik
AU  - Claire Strain-Damerell
AU  - Robin L. Owen
AU  - Martin A. Walsh
AU  - Graeme Winter
TI  - xia2.multiplex: a multi-crystal data analysis pipeline
AID  - 10.1101/2022.01.17.476589
DP  - 2022 Jan 01
TA  - bioRxiv
PG  - 2022.01.17.476589
4099  - http://biorxiv.org/content/early/2022/01/18/2022.01.17.476589.short
4100  - http://biorxiv.org/content/early/2022/01/18/2022.01.17.476589.full
AB  - In macromolecular crystallography radiation damage limits the amount of data that can be collected from a single crystal. It is often necessary to merge data sets from multiple crystals, for example small-wedge data collections on micro-crystals, in situ room-temperature data collections, and collection from membrane proteins in lipidic mesophase. Whilst indexing and integration of individual data sets may be relatively straightforward with existing software, merging multiple data sets from small wedges presents new challenges. Identification of a consensus symmetry can be problematic, particularly in the presence of a potential indexing ambiguity. Furthermore, the presence of non-isomorphous or poor-quality data sets may reduce the overall quality of the final merged data set.To facilitate and help optimise the scaling and merging of multiple data sets, we developed a new program, xia2.multiplex, which takes data sets individually integrated with DIALS and performs symmetry analysis, scaling and merging of multi-crystal data sets. xia2.multiplex also performs analysis of various pathologies that typically affect multi-crystal data sets, including non-isomorphism, radiation damage and preferential orientation. After describing a number of use cases, we demonstrate the benefit of xia2.multiplex within a wider autoprocessing framework in facilitating a multi-crystal experiment collected as part of in situ room-temperature fragment screening experiments on the SARS-CoV-2 main protease.Competing Interest StatementThe authors have declared no competing interest.