6533b821fe1ef96bd127c1c9
RESEARCH PRODUCT
Human neuroglobin: crystals and preliminary X-ray diffraction analysis
Marco NardiniThorsten BurmesterLuc MoensSylvia DewildeMartino BolognesiPaolo AscenziThomas HankelnAlessandra Pescesubject
chemistry.chemical_classificationCrystallographyProtein moleculesResolution (electron density)HexacoordinateNeuroglobinNerve Tissue ProteinsGeneral MedicineBiologymedicine.disease_causeRecombinant ProteinsAmino acidGlobinsCrystalCrystallographychemistryX-Ray DiffractionStructural BiologyNeuroglobinX-ray crystallographymedicineHumansEscherichia colidescription
Neuroglobin, a recently discovered member of the haemoglobin superfamily, is primarily expressed in the brain of humans and other vertebrates, where it has been proposed to enhance O(2) supply in response to hypoxia or ischaemia, protecting the neuron from hypoxic injury. Neuroglobin is the first example of a vertebrate haemoglobin in which a hexacoordinate haem geometry has been detected. A triple mutant (replacing three Cys residues) of human neuroglobin (151 amino acids) has been expressed in Escherichia coli, purified and crystallized in two crystal forms, the best of which diffracts to 1.95 A resolution using synchrotron radiation. The crystals belong to space group P2(1), with unit-cell parameters a = 39.6, b = 94.9, c = 67.5 A, beta = 94.4 degrees, and contain 2-4 protein molecules per asymmetric unit.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-01-01 |