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Purification, crystallization and preliminary X-ray analysis of L-sorbose reductase from Gluconobacter frateurii complexed with L-sorbose or NADPH.


ABSTRACT: NADPH-dependent L-sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with L-sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR-L-sorbose complex and the SR-NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR-L-sorbose complex belonged to space group C222(1), with unit-cell parameters a = 124.2, b = 124.1, c = 60.8 A. The crystal of the SR-NADPH complex belonged to space group P2(1), with unit-cell parameters a = 124.3, b = 61.0, c = 124.5 A, beta = 89.99 degrees . The crystals contained two and eight molecules, respectively, in the asymmetric unit.

SUBMITTER: Kubota K 

PROVIDER: S-EPMC2688410 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of L-sorbose reductase from Gluconobacter frateurii complexed with L-sorbose or NADPH.

Kubota Keiko K   Nagata Koji K   Miyazono Ken-ichi K   Toyama Hirohide H   Matsushita Kazunobu K   Tanokura Masaru M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090522 Pt 6


NADPH-dependent L-sorbose reductase (SR) from Gluconobacter frateurii was expressed in Escherichia coli, purified and crystallized with L-sorbose or NADPH using the sitting-drop vapour-diffusion method at 293 K. Crystals of the SR-L-sorbose complex and the SR-NADPH complex were obtained using reservoir solutions containing PEG 2000 or PEG 400 as precipitants and diffracted X-rays to 2.38 and 1.90 A resolution, respectively. The crystal of the SR-L-sorbose complex belonged to space group C222(1),  ...[more]

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