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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Hilgenfeld et al. (1984) studied this question.
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