1y8h

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Image:1y8h.gif

1y8h, resolution 3.10Å

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HORSE METHEMOGLOBIN LOW SALT, PH 7.0

Overview

A new relaxed state has been characterized in the crystals of horse, methemoglobin grown at neutral pH at low ionic concentration and their low, humidity variants. The crystals provide an example for improvement in, X-ray diffraction quality with reduced solvent content. Only the classical, R state has been so far observed in liganded horse hemoglobin. The state, characterized in the present study lies in between the R state and the R2, state characterized earlier in liganded human hemoglobin. The results, presented here, along with those of earlier studies, suggest that relaxed, and tense hemoglobin can access ensembles of states.

About this Structure

1Y8H is a Protein complex structure of sequences from Equus caballus with HEM as ligand. Full crystallographic information is available from OCA.

Reference

A new relaxed state in horse methemoglobin characterized by crystallographic studies., Sankaranarayanan R, Biswal BK, Vijayan M, Proteins. 2005 Aug 15;60(3):547-51. PMID:15887226

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