The structures of deoxy human haemoglobin and the mutant Hb Tyralpha42His at 120 K.
The structures of deoxy human haemoglobin and an artificial mutant (Tyralpha42-->His) have been solved at 120 K. While overall agreement between these structures and others in the PDB is very good, certain side chains are found to be shifted, absent from the electron-density map or in different rotamers. Non-crystallographic symmetry (NCS) is very well obeyed in the native protein, but not around the site of the changed residue in the mutant. NCS is also not obeyed by the water molecule invariably found in the alpha-chain haem pocket in room-temperature crystal structures of haemoglobin. At 120 K, this water molecule disappears from one alpha chain in the asymmetric unit but not the other.
Protonic Nanomachine Project, ERATO, 3-4 Hikaridai, Seika, Kyoto 619-0237, Japan. jtame@npn.jst.go.jp.
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JR
Tame
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Vallone
D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D006454:Hemoglobins / Q000737:chemistry* / Q000235:genetics; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D009154:Mutation; D011487:Protein Conformation; D014443:Tyrosine / Q000737:chemistry*
D006454:Hemoglobins; D014443:Tyrosine; D006639:Histidine; C100003:deoxyhemoglobin