6533b7d9fe1ef96bd126c34a
RESEARCH PRODUCT
New insight into the haemoglobin superfamily: preliminary crystallographic characterization of human cytoglobin.
Martino BolognesiAlessandra PesceDaniele De SanctisLuc MoensSylvia DewildePaolo AscenziThomas HankelnThorsten Burmestersubject
MutationBinding SitesMolecular StructureIronCytoglobinResolution (electron density)CytoglobinMutation MissenseGeneral MedicineBiologyCrystallography X-Raymedicine.disease_causeGlobinsCrystallographyStructural BiologymedicineHumansMoleculeOrthorhombic crystal systemGlobinBinding siteCrystallizationEscherichia colidescription
Human cytoglobin, present in almost all tissue types, is a newly identified member of the Hb superfamily. A double mutant, having both cysteines replaced by serines, has been overexpressed in Escherichia coli, purified and crystallized. A highly redundant SAD data set has been collected at the haem Fe-atom absorption edge (lambda = 1.720 A) to 2.60 A resolution. The crystals belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 46.8, b = 73.1, c = 98.9 A and two molecules per asymmetric unit. The anomalous difference Patterson map clearly reveals the position of the haem Fe-atom sites, thus paving the way for SAD structure determination.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-01-01 |