Preliminary X-ray crystallographic analysis of thermolysin in the presence of 4 <i>M</i> NaCl

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Abstract

<jats:p>The activity of thermolysin (EC 3.4.24.27) is greatly enhanced by high concentrations of neutral salts. For instance, 4 <jats:italic>M</jats:italic> NaCl enhances the activity 13–15-fold [Holmquist & Vallée (1976), <jats:italic>Biochemistry</jats:italic>, <jats:bold>15</jats:bold>, 101–107; Inouye (1992), <jats:italic>J. Biochem. (Tokyo)</jats:italic>, <jats:bold>112</jats:bold>, 335–340]. To clarify the structural basis of the activation of thermolysin by high concentrations of NaCl, we have developed a new method to introduce 4 <jats:italic>M</jats:italic> NaCl into the <jats:italic>P</jats:italic>6<jats:sub>1</jats:sub>22 crystal of thermolysin originally grown without NaCl. The crystal obtained by this method diffracted X-rays to 2.43 Å. No unit-cell parameter change was observed except the length of the <jats:italic>c</jats:italic> axis, which was elongated by 9.6% by the introduction of 4 <jats:italic>M</jats:italic> NaCl.</jats:p>

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