Crystallization and preliminary crystallographic investigation of methanol dehydrogenase from Methylobacterium extorquens AM1
Single crystals of methanol dehydrogenase (MDH) from Methylobacterium extorquens AM1 have been grown by the vapour diffusion method. These crystals diffract to beyond 2 Å resolution and are suitable for X-ray crystallography. They belong to the orthorhombic space group P2 1 2 1 2 1 and have the foll...
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Veröffentlicht in: | Journal of molecular biology 1992-11, Vol.228 (1), p.302-305 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Single crystals of methanol dehydrogenase (MDH) from
Methylobacterium extorquens AM1 have been grown by the vapour diffusion method. These crystals diffract to beyond 2 Å resolution and are suitable for X-ray crystallography. They belong to the orthorhombic space group
P2
1
2
1
2
1 and have the following unit cell parameters:
a = 66.79
A
̊
, b = 108.9
A
̊
, c = 188.9
A
̊
. One asymmetric unit contains an
α
2
β
2 tetramer of MDH and the location of the non-crystallographic 2-fold symmetry axis of this tetramer is defined by the paired positions of the binding sites of heavy atoms in four MDH-derivatives. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1016/0022-2836(92)90509-I |