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Crystallization and preliminary X‐ray diffraction studies of a bacterial flavohemoglobin protein

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Ermler, U., Siddiqui, R. A., Cramm, R., Schröder, D., & Friedrich, B. (1995). Crystallization and preliminary X‐ray diffraction studies of a bacterial flavohemoglobin protein. Proteins: Structure, Function, and Bioinformatics, 21(4), 351-353. doi:10.1002/prot.340210408.


Cite as: http://hdl.handle.net/21.11116/0000-0007-6EA7-2
Abstract
A flavohemoglobin protein (FHP) was isolated from Alcaligenes eutrophus and has been crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the FAD‐ and heme‐containing protein belong to the monoclinic space group P21 with unit cell parameters of 52.2 Å, 85.8 Å, 103.9 Å, and 81.8° corresponding to two molecules per asymmetric unit. The crystals diffract at least to a resolution of 2.0 Å and are suitable for an X‐ray structure analysis