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Acta Crystallogr D Biol Crystallogr 1995 Sep 01;51Pt 5:760-6. doi: 10.1107/S0907444995001491.
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X-ray structure determination of a dimeric hemoglobin from Caudina arenicola.

Mitchell DT , Ernst SR , Hackert ML .

The X-ray structure of a dimeric, cyanomet-liganded hemoglobin D-chain (Hb-D) from Caudina arenicola has been determined by the molecular-replacement method. The search model was a concatenated model of three hemoglobin structures superimposed on the backbone of monomeric, hemichrome hemoglobin C-chain (Hb-C) from the same organism. Hb-D crystallizes in space group P4(1)2(1)2 with cell constants a = b = 77.0 and c =61.5 A with one subunit in the asymmetric unit. The dimer twofold axis corresponds to a crystallographic twofold along one of the body diagonals of the unit cell. Rotation and translation searches as well as model refinement were carried out in X-PLOR with the final model having an R value of 0.19 using the data from 5.0 to 2.9 A resolution (R = 0.26 for 10.0 to 2.9 A resolution). The homodimeric structure of Caudina Hb-D features close heme-heme contacts with an Fe-Fe distance of 19.0 A. The subunit-subunit interface involves both the E and F helices from each subunit with the E helices oriented antiparallel at 50 degrees with respect to one another, similar to the quaternary structure observed for the homodimeric hemoglobin from Scapharca inaequivalvis.

PubMed ID: 15299806
Article link: Acta Crystallogr D Biol Crystallogr

Genes referenced: LOC115919910