Purification, crystallization, and preliminary x-ray diffraction studies of the 
flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607

Moore, Melissa J.; Distefano, Mark D.; Walsh, Christopher T.; Schiering, Nikolaus; Pai, Emil F.

doi:10.1016/S0021-9258(18)71690-6

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Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607

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Schiering, Nikolaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Pai, Emil F.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Moore, M. J., Distefano, M. D., Walsh, C. T., Schiering, N., & Pai, E. F. (1989). Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607. The Journal of Biological Chemistry, 264(24), 14386-14388. doi:10.1016/S0021-9258(18)71690-6.

Cite as: https://hdl.handle.net/21.11116/0000-000B-5EC9-A

Abstract

The flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607 was purified by dye-ligand affinity chromatography. The protein was crystallized from solutions of high ionic strength, and one of the two crystal forms obtained has proven suitable for x-ray diffraction studies. Preliminary analysis showed that these crystals belong to the tetragonal space group 1422. The unit cell dimensions are a = b = 180.7 A; c = 127.9 A. The diffraction pattern extends to better than 3 A resolution. Crystal density measurements are consistent with one enzyme dimer of 2 x 69,000 Da comprising the asymmetric unit. Trypsin treatment of the native enzyme resulted in the removal of 157 amino acids at the N terminus. After purification, the remaining fragment (amino acids 158-631), which is still fully active in vitro, could be crystallized under the same conditions as native enzyme. Twinning problems, however, did not allow complete analysis of these crystals.