Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii

AJ Schierbeek; JM van der Laan; H Groendijk; RK Wierenga; J  Drenth

doi:10.1016/s0022-2836(83)80221-6

Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii

AJ Schierbeek^*, JM van der Laan, H Groendijk, RK Wierenga, J Drenth

^*Corresponding author for this work

Research output: Contribution to journal › Letter › Academic › peer-review

11 Citations (Scopus)

Abstract

The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P212121 with one dimer in the asymmetric unit. The cell dimensions are: a = 64·2, b = 83·8, c = 193 Å. X-ray reflections extend to at least 2·2 Å resolution.

Original language	English
Pages (from-to)	563-564
Number of pages	2
Journal	Journal of Molecular Biology
Volume	165
Issue number	3
DOIs	https://doi.org/10.1016/s0022-2836(83)80221-6
Publication status	Published - 1983

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@article{c17f54e68b9041078e0c2cdc8eda0208,

title = "Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii",

abstract = "The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P212121 with one dimer in the asymmetric unit. The cell dimensions are: a = 64·2, b = 83·8, c = 193 {\AA}. X-ray reflections extend to at least 2·2 {\AA} resolution.",

author = "AJ Schierbeek and {van der Laan}, JM and H Groendijk and RK Wierenga and J Drenth",

year = "1983",

doi = "10.1016/s0022-2836(83)80221-6",

language = "English",

volume = "165",

pages = "563--564",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "3",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii

AU - Schierbeek, AJ

AU - van der Laan, JM

AU - Groendijk, H

AU - Wierenga, RK

AU - Drenth, J

PY - 1983

Y1 - 1983

N2 - The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P212121 with one dimer in the asymmetric unit. The cell dimensions are: a = 64·2, b = 83·8, c = 193 Å. X-ray reflections extend to at least 2·2 Å resolution.

AB - The FAD-containing enzyme lipoamide dehydrogenase (EC 1.6.4.3. NADH: lipoamide oxidoreductase) of Azotobacter vinelandii has been crystallized from polyethylene glycol solutions. The space group is P212121 with one dimer in the asymmetric unit. The cell dimensions are: a = 64·2, b = 83·8, c = 193 Å. X-ray reflections extend to at least 2·2 Å resolution.

U2 - 10.1016/s0022-2836(83)80221-6

DO - 10.1016/s0022-2836(83)80221-6

M3 - Letter

SN - 0022-2836

VL - 165

SP - 563

EP - 564

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii

Abstract

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