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• W2523032011 abstract "Nonribosomal peptide synthetases (NRPSs) are multimodular enzymes that synthesize a myriad of diverse molecules. Tailoring domains have been co-opted into NRPSs to introduce further variety into nonribosomal peptide products. Linear gramicidin synthetase contains a unique formylation-tailoring domain in its initiation module (F-A-PCP). The structure of the F-A di-domain has previously been determined in a crystal form which had large solvent channels and no density for the minor A sub subdomain. An attempt was made to take advantage of this packing by removing the A sub subdomain from the construct (F-A Δsub ) in order to produce a crystal that could accommodate the PCP domain. In the resulting crystal the original packing network was still present, but a second network with the same packing and almost no contact with the original network took the place of the solvent channels and changed the space group of the crystal." @default.
• W2523032011 created "2016-09-30" @default.
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• W2523032011 date "2016-09-20" @default.
• W2523032011 modified "2023-09-27" @default.
• W2523032011 title "Manipulation of an existing crystal form unexpectedly results in interwoven packing networks with pseudo-translational symmetry" @default.
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• W2523032011 doi "https://doi.org/10.1107/s2059798316013504" @default.
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