The mutated hemoglobin HbC (β6 Glu→ Lys), in the oxygenated (R) liganded state, forms
crystals inside red blood cells of patients with CC and SC diseases. Static and dynamic light …

Crystallization of the mutated hemoglobin, HbC, which occurs inside red blood cells of
patients expressing β C-globin and exhibiting the homozygous CC and the heterozygous …

Five crystal forms of the abnormal human hemoglobin Hb‡ C (beta six Glu→ Lys) have been
grown. Two of them are grown with liganded Hb C, three with deoxy Hb C. The structures of …

We previously reported that circulating hemoglobin (Hb) CC erythrocytes contain
oxygenated HbC crystals with little or no HbF and that HbF inhibits in vitro crystallization of …

The liganded hemoglobin (Hb) high-salt crystallization condition described by Max Perutz
has generated three different crystals of human adult carbonmonoxy hemoglobin (COHbA) …

Based upon existing crystallographic evidence, HbS, HbC, and HbA have essentially the
same molecular structure. However, important areas of the molecule are not well defined …

Hemoglobin C (Glu β6→ Lys) shares with hemoglobin S (Glu β6→ Val) the site of mutation,
but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms …

The fundamental pathophysiology of sickle cell disease is predicated by the polymerization
of deoxygenated (T-state) sickle hemoglobin (Hb S) into fibers that distort red blood cells into …

Recent crystallographic studies suggested that fully liganded human hemoglobin can adopt
multiple quaternary conformations that include the two previously solved relaxed …

Reversible liquid-liquid (LL) phase separation in the form of high concentration hemoglobin
(Hb) solution droplets is favored in an equilibrium with a low-concentration Hb solution when …