Human neuroglobin: crystals and preliminary X-ray diffraction analysis

被引:17
作者
Pesce, A
Nardini, M
Dewilde, S
Ascenzi, P
Burmester, T
Hankeln, T
Moens, L
Bolognesi, M
机构
[1] Univ Genoa, Dept Phys, INFM, I-16146 Genoa, Italy
[2] Univ Genoa, Ctr Excellence Biomed Res, I-16146 Genoa, Italy
[3] Univ Instelling Antwerp, Dept Biochem, B-2610 Antwerp, Belgium
[4] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy
[5] Johannes Gutenberg Univ Mainz, Inst Zool, D-55099 Mainz, Germany
[6] Johannes Gutenberg Univ Mainz, Inst Mol Genet, D-55099 Mainz, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
D O I
10.1107/S090744490201260X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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 Angstrom, beta = 94.4degrees, and contain 2-4 protein molecules per asymmetric unit.
引用
收藏
页码:1848 / 1850
页数:3
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