Purification and crystallization of recombinant Escherichia coli malate dehydrogenase

Michael D. Hall; David G. Levitt; Lee McAllister-Henn; Leonard J. Banaszak

doi:10.1016/0022-2836(91)90099-R

Purification and crystallization of recombinant Escherichia coli malate dehydrogenase

Michael D. Hall, David G. Levitt, Lee McAllister-Henn, Leonard J. Banaszak

Physiology

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C222₁ form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 Å has been collected.

Original language	English (US)
Pages (from-to)	551-553
Number of pages	3
Journal	Journal of Molecular Biology
Volume	220
Issue number	3
DOIs	https://doi.org/10.1016/0022-2836(91)90099-R
State	Published - Aug 5 1991

Bibliographical note

Funding Information:
The eMDH project was supported by the National Science Foundation, U.S.A. (L.J.B., DNB 8941746) and the NTH (T,.M.-H., GM33218).

Keywords

MDH
MDHase
citric acid cycle
dehydrogenase
malate dehydrogenase

Publisher link

10.1016/0022-2836(91)90099-R

Find It

Find It at U of M Libraries

Cite this

@article{2c3fba5f36bb4d1ea4eb998b46a255f5,

title = "Purification and crystallization of recombinant Escherichia coli malate dehydrogenase",

abstract = "Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C2221 form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 {\AA} has been collected.",

keywords = "MDH, MDHase, citric acid cycle, dehydrogenase, malate dehydrogenase",

author = "Hall, {Michael D.} and Levitt, {David G.} and Lee McAllister-Henn and Banaszak, {Leonard J.}",

note = "Funding Information: The eMDH project was supported by the National Science Foundation, U.S.A. (L.J.B., DNB 8941746) and the NTH (T,.M.-H., GM33218).",

year = "1991",

month = aug,

day = "5",

doi = "10.1016/0022-2836(91)90099-R",

language = "English (US)",

volume = "220",

pages = "551--553",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Purification and crystallization of recombinant Escherichia coli malate dehydrogenase

AU - Hall, Michael D.

AU - Levitt, David G.

AU - McAllister-Henn, Lee

AU - Banaszak, Leonard J.

N1 - Funding Information: The eMDH project was supported by the National Science Foundation, U.S.A. (L.J.B., DNB 8941746) and the NTH (T,.M.-H., GM33218).

PY - 1991/8/5

Y1 - 1991/8/5

N2 - Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C2221 form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 Å has been collected.

AB - Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C2221 form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 Å has been collected.

KW - MDH

KW - MDHase

KW - citric acid cycle

KW - dehydrogenase

KW - malate dehydrogenase

UR - http://www.scopus.com/inward/record.url?scp=0025886175&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025886175&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(91)90099-R

DO - 10.1016/0022-2836(91)90099-R

M3 - Article

C2 - 1870122

AN - SCOPUS:0025886175

VL - 220

SP - 551

EP - 553

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -

Purification and crystallization of recombinant Escherichia coli malate dehydrogenase

Abstract

Bibliographical note

Keywords

Publisher link

Find It

Other files and links

Fingerprint

Cite this