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

^*Corresponding author for this work

Institute of Biochemistry

15 Citations (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.

Original language	English
Journal	FEBS Letters
Volume	170
Issue number	1
Pages (from-to)	143-146
Number of pages	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(84)81387-3
Publication status	Published - 07.05.1984

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0014-5793(84)81387-3

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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.",

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AU - Hilgenfeld, R.

AU - Saenger, W.

AU - Schomburg, U.

AU - Krauss, G.

PY - 1984/5/7

Y1 - 1984/5/7

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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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ER -

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

Abstract

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UN SDGs

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