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 | |
| Publication status | Published - 07.05.1984 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
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