Novel crystal forms of a proteolytic core of the single-stranded DNA-binding protein (SSB) from E. coli

R. Hilgenfeld; W. Saenger; U. Schomburg; G. Krauss

doi:10.1016/0014-5793(84)81387-3

Novel crystal forms of a proteolytic core of the single-stranded DNA-binding protein (SSB) from E. coli

R. Hilgenfeld, W. Saenger^*, U. Schomburg, G. Krauss

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

15 Zitate (Scopus)

Abstract

A proteolytic core of the Escherichia coli single-stranded DNA-binding protein (SSB) has been crystallized from phosphate buffer. Crystals suitable for X-ray data collection display monoclinic space group C2 with α = 106.8, b = 62.3 c = 100.2 Å, β = 112° and contain one tetramer of proteolysis product SSB*-A per asymmetric unit. Two other crystal forms have been obtained in the presence of the inhibitor diisopropylfluorophosphate.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	170
Ausgabenummer	1
Seiten (von - bis)	143-146
Seitenumfang	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(84)81387-3
Publikationsstatus	Veröffentlicht - 07.05.1984

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10.1016/0014-5793(84)81387-3

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title = "Novel crystal forms of a proteolytic core of the single-stranded DNA-binding protein (SSB) from E. coli",

abstract = "A proteolytic core of the Escherichia coli single-stranded DNA-binding protein (SSB) has been crystallized from phosphate buffer. Crystals suitable for X-ray data collection display monoclinic space group C2 with α = 106.8, b = 62.3 c = 100.2 {\AA}, β = 112° and contain one tetramer of proteolysis product SSB*-A per asymmetric unit. Two other crystal forms have been obtained in the presence of the inhibitor diisopropylfluorophosphate.",

author = "R. Hilgenfeld and W. Saenger and U. Schomburg and G. Krauss",

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AU - Hilgenfeld, R.

AU - Saenger, W.

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AU - Krauss, G.

PY - 1984/5/7

Y1 - 1984/5/7

N2 - A proteolytic core of the Escherichia coli single-stranded DNA-binding protein (SSB) has been crystallized from phosphate buffer. Crystals suitable for X-ray data collection display monoclinic space group C2 with α = 106.8, b = 62.3 c = 100.2 Å, β = 112° and contain one tetramer of proteolysis product SSB*-A per asymmetric unit. Two other crystal forms have been obtained in the presence of the inhibitor diisopropylfluorophosphate.

AB - A proteolytic core of the Escherichia coli single-stranded DNA-binding protein (SSB) has been crystallized from phosphate buffer. Crystals suitable for X-ray data collection display monoclinic space group C2 with α = 106.8, b = 62.3 c = 100.2 Å, β = 112° and contain one tetramer of proteolysis product SSB*-A per asymmetric unit. Two other crystal forms have been obtained in the presence of the inhibitor diisopropylfluorophosphate.

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DO - 10.1016/0014-5793(84)81387-3

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Novel crystal forms of a proteolytic core of the single-stranded DNA-binding protein (SSB) from E. coli

Abstract

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