Extracellular Endonuclease of Serratia marcescens.
1. Three-Dimensional Structure of Crystalline Protein
at 1.7 Resolution

V. Yu. Lunin¹, E. V. Blagova², V. M. Levdikov², V. V. Lunin², S. V. Shlyapnikov³,
M. Perbandt⁴, K. S. Raishankar⁴, H. Betzel⁴, and A. M. Mikhailov²

¹ Institute of Mathematical Problems in Biology, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia
² Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow, 117333 Russia;
E-mail: amm@biostr.crystal.msk.ru
³ Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 117984 Russia
⁴ Institute of Physiological Chemistry, Hamburg University, Hamburg, 22603 Germany

Received February 16, 1998

Abstract—A refined crystal structure of Serratia marcescens nuclease is reported to an R factor of 17.3% and
R_free factor of 22.2% at a 1.7 Å resolution. The structure includes 3678 nonhydrogen atoms of the enzyme and
443 bound water molecules. The average deviations of bond lengths and valent angles from their standard val-
ues are 0.011 Å and 1.8°, and the maximal deviations are 0.07 Å and 11°, respectively. A new topological model
of the enzyme molecule is proposed, indicating high symmetry of the monomer in its N- and C-terminal
regions.

Key words: Serratia marcescens, extracellular endonuclease, X-ray crystallography, atomic structure

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