PMID:11807277
| Citation |
Abad, MC, Binderup, K, Preiss, J and Geiger, JH (2002) Crystallization and preliminary X-ray diffraction studies of Escherichia coli branching enzyme. Acta Crystallogr. D Biol. Crystallogr. 58:359-61 |
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| 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. |
| Links | |
| Keywords |
1,4-alpha-Glucan Branching Enzyme/chemistry; 1,4-alpha-Glucan Branching Enzyme/metabolism; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Protein Conformation; Selenomethionine/chemistry |
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