title: Overexpression, purification and crystallization of BamHI endonuclease.
abstract: The type II restriction endonuclease BamHI has been expressed in E. coli, producing 100-fold more enzyme than the wild type Bacillus amyloliquefaciens H strain. This high yield has facilitated purification to homogeneity of large amounts of the enzyme, along with its crystallization in a form which diffracts to at least 1.9 A in X-ray analysis.
authors.affiliation: New England Biolabs, Inc., Beverly, MA 01915.
authors.forename: W E
authors.initials: WE
authors.lastname: Jack
authors.forename: L
authors.initials: L
authors.lastname: Greenough
authors.forename: L F
authors.initials: LF
authors.lastname: Dorner
authors.forename: S Y
authors.initials: SY
authors.lastname: Xu
authors.forename: T
authors.initials: T
authors.lastname: Strzelecka
authors.forename: A K
authors.initials: AK
authors.lastname: Aggarwal
authors.forename: I
authors.initials: I
authors.lastname: Schildkraut
mesh_terms: D001407:Bacillus / Q000201:enzymology; D003001:Cloning, Molecular; D003460:Crystallization; D015245:Deoxyribonuclease BamHI / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D015245:Deoxyribonuclease BamHI