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   <subfield code="a">Crystal Structure Determination of a Flavoprotein FP390 from a Luminescent Bacterium, Photobacterium phosphoreum</subfield>
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   <subfield code="c">[Akiko Kita, Sabu Kasai, Kunio Miki]</subfield>
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   <subfield code="a">The three-dimensional structure of a flavoprotein, FP390, purified from a luminescent bacterium, Photobacterium phosphoreum, has been determined at 3 Â resolution by X-ray crystallography. Crystallographic refinements of the structural model have led to an R-factor of 0.24 for the intensity data between 6 to 3 Â resolution collected with synchrotron radiation. It was found that a homodimer of the FP390 molecules related by a non-crystallo-graphic 2-fold axis is comprised in the asymmetric unit. Two homodimers are arranged around a crystallographic 2-fold axis to form a tetrameric assembly. The monomer molecule of FP390, to which two molecules of the flavin cofactor (Q-flavin) are bound, consists of a seven-stranded parallel β-sheet which forms a half of the β-barrel structure and seven α-helices which surround one side of the β-barrel. We suggest that the reason why the Q-flavin sample prepared from FP390 is always a mixture of two components is connected with the fact that the monomer molecules has two flavin binding sites, at the dimer interface and at the molecular surface.</subfield>
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