8RGS

Serial synchrotron in plate room temperature structure of Dye Type Peroxidase Aa

Summary for 8RGS

• Entry DOI: 10.2210/pdb8rgs/pdb
• Related: 8RGS 8RGW
• Descriptor: Deferrochelatase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: serial synchrotron crystallography, heme peroxidase, metalloproteins, oxidoreductase
• Biological source: Streptomyces lividans
• Total number of polymer chains: 2
• Total formula weight: 81713.01

Authors

Thompson, A.J.,Hough, M.A.,Williams, L.J.,Worrall, J.A.R.,Sanchez-Weatherby, J.,Mikolajek, H.,Sandy, J. (deposition date: 2023-12-14, release date: 2023-12-27, Last modification date: 2024-04-17)

Primary citation

Thompson, A.J.,Sanchez-Weatherby, J.,Williams, L.J.,Mikolajek, H.,Sandy, J.,Worrall, J.A.R.,Hough, M.A.
Efficient in situ screening of and data collection from microcrystals in crystallization plates.
Acta Crystallogr D Struct Biol, 80:279-288, 2024

PubMed Abstract: A considerable bottleneck in serial crystallography at XFEL and synchrotron sources is the efficient production of large quantities of homogenous, well diffracting microcrystals. Efficient high-throughput screening of batch-grown microcrystals and the determination of ground-state structures from different conditions is thus of considerable value in the early stages of a project. Here, a highly sample-efficient methodology to measure serial crystallography data from microcrystals by raster scanning within standard in situ 96-well crystallization plates is described. Structures were determined from very small quantities of microcrystal suspension and the results were compared with those from other sample-delivery methods. The analysis of a two-dimensional batch crystallization screen using this method is also described as a useful guide for further optimization and the selection of appropriate conditions for scaling up microcrystallization.

PubMed: 38488731
DOI: 10.1107/S2059798324001955

Experimental method

X-RAY DIFFRACTION (1.79 Å)