title: Crystallization and preliminary X-ray diffraction studies of Escherichia coli branching enzyme.
abstract: Branching enzyme catalyzes the formation of the branch points in glycogen and starch by cleavage of the alpha-1,4 link and its subsequent transfer to the alpha-1,6 position. This paper reports the crystallization and preliminary structural studies of an amino-terminally truncated branching enzyme from Escherichia coli. High-resolution diffracting crystals were obtained and a complete native data set to a resolution of 2.3 A was collected. These crystals belong to the P2(1) space group, with unit-cell parameters a = 91.44, b = 102.58, c = 185.41 A, beta = 91.38 degrees. A native data set with 99.6% completeness, an overall R(merge) of 0.086 and I/sigma(I) of 10.43 was obtained.
authors.affiliation: Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.
authors.forename: Marta C
authors.initials: MC
authors.lastname: Abad
authors.forename: Kim
authors.initials: K
authors.lastname: Binderup
authors.forename: Jack
authors.initials: J
authors.lastname: Preiss
authors.forename: James H
authors.initials: JH
authors.lastname: Geiger
mesh_terms: D015061:1,4-alpha-Glucan Branching Enzyme / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D012645:Selenomethionine / Q000737:chemistry
chemical_list: D012645:Selenomethionine; D015061:1,4-alpha-Glucan Branching Enzyme