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June 2024 issue
Cover illustration: Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO [Bjelcic et al. (2024), Acta Cryst. F80, 117–124]. RuBisCO is the enzyme responsible for the first step of carbon dioxide fixation in plants, and this reaction is of enormous importance in agriculture and the environment. The results presented provide a good starting point for time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
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The first room-temperature serial crystallography structure of RuBisCO is presented.
RSF1 changes the chromatin-remodeling mode of SNF2h. The RSF complex does not have a nucleosome-recentering capacity and a `critical distance' exists during the action of RSF in vitro; this distance is about 24 base pairs. The RSF complex loosens parts of the nucleosome DNA and undergoes conformational change on linker DNA stimulation.
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