The 1.6A Structure of Horse Methemoglobin at pH 7.1

A pH-Dependent Aquomet-to-Hemichrome Transition in Crystalline Horse Methemoglobin

An X-Ray Study of Horse Methaemoglobin. I

The Structure of Haemoglobin. III. Direct Determination of the Molecular Transform

VLSAADKTNVKAAWSKVGGHAGEYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGAL
SDLSNLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSSVSTVLTSKYR

VQLSGEEKAAVLALWDKVNEEEVGGEALGRLLVVYPWTQRFFDSFGDLSNPGAVMGNPKVKAHGKKVLHSFGEGVHHLDN
LKGTFAALSELHCDKLHVDPENFRLLGNVLVVVLARHFGKDFTPELQASYQKVVAGVANALAHKYH

1.5M ammonium sulfate, 0.35 M ammonium phosphate, pH 7.1, VAPOR DIFFUSION, temperature 298K

Partnering equine alpha hemichrome/ beta aquomet hemoglobin structure at pH 5.4

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

The biological assembly (tetramer) is generated from the dimer in the asymetric unit bu the operation: -x, y, -z

aquomet hemoglobin, globin fold, bisimidazole at low pH, OXYGEN STORAGE-TRANSPORT COMPLEX

VLSAADKTNVKAAWSKVGGHAGEYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTLAVGHLDDLPGAL
SNLSDLHAHKLRVDPVNFKLLSHCLLSTLAVHLPNDFTPAVHASLDKFLSSVSTVLTSKYR