Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis

S J  Charnock; G J  Davies

Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis

Chemistry

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

Abstract

Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and overexpressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C222(1), with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 Angstrom and with one molecule of spsA. in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.

Original language	English
Pages (from-to)	677-678
Number of pages	2
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	55
Publication status	Published - Mar 1999

Keywords

SPORULATION

Cite this

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title = "Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis",

abstract = "Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and overexpressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C222(1), with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 Angstrom and with one molecule of spsA. in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.",

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author = "Charnock, {S J} and Davies, {G J}",

year = "1999",

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language = "English",

volume = "55",

pages = "677--678",

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

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T1 - Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis

AU - Charnock, S J

AU - Davies, G J

PY - 1999/3

Y1 - 1999/3

N2 - Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and overexpressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C222(1), with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 Angstrom and with one molecule of spsA. in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.

AB - Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and overexpressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C222(1), with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 Angstrom and with one molecule of spsA. in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.

KW - SPORULATION

M3 - Article

SN - 0907-4449

VL - 55

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EP - 678

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

ER -