TY - JOUR
T1 - Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe‐2S] centers
AU - Romão, Maria J.
AU - Barata, Belarmino A. S.
AU - Archer, Margarida
AU - Lobeck, Karin
AU - Moura, Isabel
AU - CARRONDO, Maria A.
AU - LeGall, Jean
AU - Lottspeich, Friedrich
AU - Huber, Robert
AU - Moura, José J. G.
PY - 1993/1/1
Y1 - 1993/1/1
N2 -
The Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe‐2S] centers. The enzyme was characterized by SDS/PAGE, gel‐filtration and analytical ultracentrifugation experiments. It was crystallized at 4°C, pH 7.2, using isopropanol and MgCl
2
as precipitants. The crystals diffract beyond 0.3‐nm (3.0‐Å) resolution and belong to space group P6
1
22 or its enantiomorph, with cell dimensions a=b= 14.45 nm and c= 16.32 nm. There is one subunit/asymmetric unit which gives a packing density of 2.5 × 10
−3
nm
3
/Da (2.5 Å
3
/Da), consistent with the experimental crystal density, p= 1.14 g/cm
3
. One dimer (approximately 2 × 100 kDa) is located on a crystallographic twofold axis.
AB -
The Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe‐2S] centers. The enzyme was characterized by SDS/PAGE, gel‐filtration and analytical ultracentrifugation experiments. It was crystallized at 4°C, pH 7.2, using isopropanol and MgCl
2
as precipitants. The crystals diffract beyond 0.3‐nm (3.0‐Å) resolution and belong to space group P6
1
22 or its enantiomorph, with cell dimensions a=b= 14.45 nm and c= 16.32 nm. There is one subunit/asymmetric unit which gives a packing density of 2.5 × 10
−3
nm
3
/Da (2.5 Å
3
/Da), consistent with the experimental crystal density, p= 1.14 g/cm
3
. One dimer (approximately 2 × 100 kDa) is located on a crystallographic twofold axis.
UR - http://www.scopus.com/inward/record.url?scp=0027217139&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1993.tb18085.x
DO - 10.1111/j.1432-1033.1993.tb18085.x
M3 - Article
C2 - 8354279
AN - SCOPUS:0027217139
VL - 215
SP - 729
EP - 732
JO - European Journal Of Biochemistry
JF - European Journal Of Biochemistry
SN - 0014-2956
IS - 3
ER -