Crystallographic structure of Allophycocyanin from <i>Gracilaria chilensis</i>.

<p>A) Ribbon representation of the asymmetric unit, the heterodimer. B) A section of the |2F-Fo| omit electron density map is shown for phycocyanobilin in α subunit. The residues interacting with the chromophore are also shown.</p

Structural models proposed for each trimer of Allophycocyanin.

<p>A) Schematic representation of the different composition trimers. B) Structure of APC, APC_1, APC_2, and APC_3.</p

Spectroscopic characterization and oligomerization state of Allophycocyanin.

<p>A) Absorption (-) and emission (--) spectra of purified Allophycocyanin. B) Molecular sieve chromatogram; the standards and the sample are indicated.</p

Characterization of phycobilisomes of <i>Gracilaria chilensis</i>.

<p>A) Absorption(-) and emission(..) spectra. B) Transmission electron micrograph of purified phycobilisomes.The inserts show amplified images. Schematic drawings of PBS are also shown.</p

Sequence comparison between α and α^II (ApcA and ApcD), β and β¹⁸ (Apcb and ApcF) and α and the PB_domain of the L_CM (ApcA and ApcE).

<p>Chromophore binding region are enclosed in green rectangles, and the conserved residues are highlighted in green. The cysteine residues that bind the chromophores are shown in red background. The PB-loop sequence is enclosed in blue lines.</p