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Crystallization and characterization of the recombinant human Clara cell 10‐kDa protein
Author(s) -
Matthews John H.,
Pattabiraman N.,
Ward Keith B.,
Mantile Giuditta,
Miele Lucio,
Mukherjee Anil B.
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340200209
Subject(s) - triclinic crystal system , monoclinic crystal system , polyethylene glycol , ammonium sulfate , crystallography , peg ratio , crystallization , recombinant dna , chemistry , lattice constant , crystal structure , diffraction , biochemistry , chromatography , organic chemistry , physics , finance , optics , economics , gene
Crystals of recombinant human Clara cell 10‐kDa protein were grown both from ammonium sulfate and polyethylene glycol (PEG) solutions. Crystals grown from ammonium sulfate solution have been characterized by X‐ray diffraction studies as monoclinic with the space group C 2 and lattice constants a = 69.2 Å, b = 83.0 Å, c = 58.3 Å, and β = 99.7°. The monoclinic crystals diffract to beyond 2.5 Å. Some of the crystals grown from PEG were of a similar habit to those grown from ammonium sulfate, but others were triclinic with the space group P 1 and cell constants a = 40.3 Å, b = 46.3 Å, c = 51.3 Å, α = 117.7°, β = 102.3°, and γ = 71.4°. These crystals diffract to beyond 3.2 Å. © 1994 Wiley‐Liss, Inc.