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

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

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...

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Veröffentlicht in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1995-04, Vol.21 (4), p.351-353
Hauptverfasser: Ermler, Ulrich, Siddiqui, Roman A., Cramm, Rainer, Friedrich, Bärbel, Schröder, Dirk
Format: Artikel
Sprache:eng
Schlagworte:
Alcaligenes - chemistry
Alcaligenes eutrophus
Bacterial Proteins - chemistry
Crystallization
Crystallography, X-Ray
electron transfer
flavoprotein
Flavoproteins - chemistry
hemoglobin
Hemoglobins - chemistry
protein crystallization
X‐ray crystallography
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Zusammenfassung: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. © 1995 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.340210408