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Literature summary for 1.5.1.38 extracted from

  • Gao, B.; Bertrand, A.; Boles, W.H.; Ellis, H.R.; Mallett, T.C.
    Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli (2005), Acta Crystallogr. Sect. F, 61, 837-840.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor-diffusion technique yields single crystals that grow as hexagonal rods and diffract to 2.9 A resolution using synchrotron X-ray radiation. The protein crystallizes in the primitive hexagonal space group P622. Substitution of two leucine residues (Leu114 and Leu165) to methionine is performed to obtain selenomethionine-containing SsuE for MAD phasing. The selenomethionine derivative of SsuE has been expressed and purified and crystals of the protein have been obtained with and without bound FMN Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
SsuE
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Escherichia coli