Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis

Edward Taylor; Simon Charnock; John Colby; Gideon Davies; Gary Black

doi:10.1107/S090744490100748X

Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis

Edward Taylor, Simon Charnock, John Colby, Gideon Davies, Gary Black

Applied Sciences Department

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

3 Citations (Scopus)

Abstract

The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 Å using an in-house Cu Kα source and belong to either space group P6522 or P6122, with unit-cell parameters a = b = 72.4, c = 241.2 Å, and have two molecules of YckF in the asymmetric unit.

Original language	English
Pages (from-to)	1138-1140
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	57
Issue number	8
DOIs	https://doi.org/10.1107/S090744490100748X
Publication status	Published - 2001

Keywords

carbon fixation
6-phospho-3-hexulose isomerase

Access to Document

10.1107/S090744490100748X

Cite this

@article{2bdc522e187842a7a0ffcd8e60a0ead7,

title = "Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis",

abstract = "The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 {\AA} using an in-house Cu Kα source and belong to either space group P6522 or P6122, with unit-cell parameters a = b = 72.4, c = 241.2 {\AA}, and have two molecules of YckF in the asymmetric unit.",

keywords = "carbon fixation, 6-phospho-3-hexulose isomerase",

author = "Edward Taylor and Simon Charnock and John Colby and Gideon Davies and Gary Black",

year = "2001",

doi = "10.1107/S090744490100748X",

language = "English",

volume = "57",

pages = "1138--1140",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "Blackwell Publishing",

number = "8",

}

TY - JOUR

T1 - Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis

AU - Taylor, Edward

AU - Charnock, Simon

AU - Colby, John

AU - Davies, Gideon

AU - Black, Gary

PY - 2001

Y1 - 2001

N2 - The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 Å using an in-house Cu Kα source and belong to either space group P6522 or P6122, with unit-cell parameters a = b = 72.4, c = 241.2 Å, and have two molecules of YckF in the asymmetric unit.

AB - The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 Å using an in-house Cu Kα source and belong to either space group P6522 or P6122, with unit-cell parameters a = b = 72.4, c = 241.2 Å, and have two molecules of YckF in the asymmetric unit.

KW - carbon fixation

KW - 6-phospho-3-hexulose isomerase

U2 - 10.1107/S090744490100748X

DO - 10.1107/S090744490100748X

M3 - Article

SN - 0907-4449

VL - 57

SP - 1138

EP - 1140

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 8

ER -

Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis

Abstract

Keywords

Access to Document

Fingerprint

Cite this