Crystallization of recombinant chitobiase from Serratia marcescens.
We are currently investigating the biochemical and structural properties of both chitin degrading enzymes chitinase and chitobiase from Serratia marcescens. Previously we have reported the first crystallization and characterization of chitinase crystals (Vorgias et al., 1992). In this communication we present the first crystallization of chitobiase. The protein was synthesized in Escherichia coli and purified to homogeneity using cation exchange chromatography and fast protein liquid chromatography. The crystals have the shape of small prisms and the space group is P2(1) with beta = 101.0 degrees and unit cell dimensions a = 63.2 A, b = 133.2 A, c = 55.1 A. They diffract X-rays to about 2.5 A resolution and are suitable for three-dimensional structural analysis.
Tews
I
I
European Molecular Biology Laboratory (EMBL), Hamburg, Germany.
Dauter
Z
Z
Oppenheim
A B
AB
Vorgias
C E
CE
D000118:Acetylglucosaminidase / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli; D011994:Recombinant Proteins / Q000737:chemistry; D012706:Serratia marcescens / Q000201:enzymology*; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D000118:Acetylglucosaminidase