New insight into the haemoglobin superfamily: preliminary crystallographic characterization of human cytoglobin.
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.
de Sanctis
Daniele
D
Department of Physics - INFM and Center for Excellence in Biomedical Research, University of Genova, Via Dodecaneso 33, I-16146 Genova, Italy.
Dewilde
Sylvia
S
Pesce
Alessandra
A
Ascenzi
Paolo
P
Burmester
Thorsten
T
Hankeln
Thomas
T
Moens
Luc
L
Bolognesi
Martino
M
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D000078842:Cytoglobin; D005914:Globins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D007501:Iron; D015394:Molecular Structure; D020125:Mutation, Missense
C000627265:CYGB protein, human; D000078842:Cytoglobin; D005914:Globins; D007501:Iron