Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.

The enzyme 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni was crystallized. Crystals, of up to 0.6 mm in their longest dimension and suitable for a crystallographic analysis have been obtained by the vapour diffusion method. They belong to the orthorhombic lattice type and d...

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Hauptverfasser: Benach, J, Knapp, S, Oppermann, U, Hägglund, O, Jörnvall, H, Ladenstein, R
Format: Journal article
Sprache:English
Veröffentlicht: Blackwell Publishing Ltd 1996
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author Benach, J
Knapp, S
Oppermann, U
Hägglund, O
Jörnvall, H
Ladenstein, R
author_facet Benach, J
Knapp, S
Oppermann, U
Hägglund, O
Jörnvall, H
Ladenstein, R
author_sort Benach, J
collection OXFORD
description The enzyme 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni was crystallized. Crystals, of up to 0.6 mm in their longest dimension and suitable for a crystallographic analysis have been obtained by the vapour diffusion method. They belong to the orthorhombic lattice type and diffract to a maximum resolution of 0.23 nm. A final data set obtained by merging data from three crystals resulted in a completeness of 90% with an Rmerge of 6%. A molecular replacement search carried out by using 3 alpha (or 20 beta)-hydroxysteroid dehydrogenase from Streptomyces hydrogenans as a search model allowed us to assign I222 as the correct space group and to propose a model for the crystal packing, with one monomer per asymmetric unit. Thus, the whole unit cell contains two tetramers. The R-factor after rigid body refinement is 48.1%.
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spelling oxford-uuid:eeefcc06-8473-4a80-a33c-e15fda3b30d22022-03-27T11:36:34ZCrystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:eeefcc06-8473-4a80-a33c-e15fda3b30d2EnglishSymplectic Elements at OxfordBlackwell Publishing Ltd1996Benach, JKnapp, SOppermann, UHägglund, OJörnvall, HLadenstein, RThe enzyme 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni was crystallized. Crystals, of up to 0.6 mm in their longest dimension and suitable for a crystallographic analysis have been obtained by the vapour diffusion method. They belong to the orthorhombic lattice type and diffract to a maximum resolution of 0.23 nm. A final data set obtained by merging data from three crystals resulted in a completeness of 90% with an Rmerge of 6%. A molecular replacement search carried out by using 3 alpha (or 20 beta)-hydroxysteroid dehydrogenase from Streptomyces hydrogenans as a search model allowed us to assign I222 as the correct space group and to propose a model for the crystal packing, with one monomer per asymmetric unit. Thus, the whole unit cell contains two tetramers. The R-factor after rigid body refinement is 48.1%.
spellingShingle Benach, J
Knapp, S
Oppermann, U
Hägglund, O
Jörnvall, H
Ladenstein, R
Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title_full Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title_fullStr Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title_full_unstemmed Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title_short Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
title_sort crystallization and crystal packing of recombinant 3 or 17 beta hydroxysteroid dehydrogenase from comamonas testosteroni attc 11996
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