2.9 ANGSTROM CRYSTAL STRUCTURE OF LAMPREY HEMOGLOBIN THAT HAS BEEN EXPOSED TO CARBON MONOXIDE.

Crystalline ligand transitions in lamprey hemoglobin. Structural evidence for the regulation of oxygen affinity.

The 2.7 Angstrom Crystal Structure of Deoxygentated Hemoglobin from the Sea Lamprey (Petromyzon Marinus): Structural Basis for a Lowered Oxygen Affinity and Bohr Effect.

PIVDTGSVAPLSAAEKTKIRSAWAPVYSTYETSGVDILVKFFTSTPAAQEFFPKFKGLTTADQLKKSADVRWHAERIINA
VNDAVASMDDTEKMSMKLRDLSGKHAKSFQVDPQYFKVLAAVIADTVAAGDAGFEKLMSMICILLRSAY

25% PEG 4K,
170mM phosphate buffer, pH 6.8, SMALL TUBES, temperature 296K

2.9 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED LAMPREY HEMOGLOBIN V IN THE SPACE GROUP P2(1)2(1)2(1)

2.7 Angstrom crystal structure of deoxygentated lamprey hemoglobin V in the space group p2(1) with twelve monomers in the assymetric unit.

Refinement of a molecular model for
lamprey hemoglobin from Petromyzon marinus.

Crystalline ligand transition experiments.

Simulated annealing, Powell
minimization, group
B-factor and group occupancy
refinements using tight
non-crystallographic symmetry
restraints (wa=200) on the
protein except for residue 73.

The physiologically relevent
assembly is a homodimer in
which the subunits are related
by a twofold axis of symmetry.

A hexameric assembly is
observed upon application of
crystallographic symmetry
operators. The subunits in the
hexamer are arranged as one
turn of an approximately
three-fold screw.

crystalline ligand transitions, hemoglobin, heme, lamprey, OXYGEN STORAGE-TRANSPORT COMPLEX

PIVDTGSVAPLSAAEKTKIRSAWAPVYSNYETSGVDILVKFFTSTPAAQEFFPKFKGLTTADQLKKSADVRWHAERIINA
VNDAVVSMDDTEKMSMKLRDLSGKHAKSFQVDPQYFKVLAAVIADTVAAGDAGFEKLMSMICILLRSAY