Abstract
The C-terminal 232-419 amino acids fragment of endonuclease Sau3AI has been successfully expressed in Escherichia coli with 6 His at its N-terminal. After purification and crystallization, one completed 2.8 Å data set was collected using a Rigaku R-AXIS IV ++ diffractometer. The plate-like crystals belong to orthorhombic space group P212121 with the cell dimension of a = 34.75, b = 76.82, c = 123.59Å and contain one molecule per asymmetric unit.
Keywords: Sau3AI endonuclease, crystallization, preliminary X-ray analysis
Protein & Peptide Letters
Title: Crystallization and Preliminary X-Ray Analysis of Sau3AI C-Terminal 232-419 Amino Acids Fragment
Volume: 13 Issue: 6
Author(s): Feng Yu, Jiaping Song, Chunyan Xu, Yu Ding, Xiaojian Hu, Jianhua He and Zhihong Zhang
Affiliation:
Keywords: Sau3AI endonuclease, crystallization, preliminary X-ray analysis
Abstract: The C-terminal 232-419 amino acids fragment of endonuclease Sau3AI has been successfully expressed in Escherichia coli with 6 His at its N-terminal. After purification and crystallization, one completed 2.8 Å data set was collected using a Rigaku R-AXIS IV ++ diffractometer. The plate-like crystals belong to orthorhombic space group P212121 with the cell dimension of a = 34.75, b = 76.82, c = 123.59Å and contain one molecule per asymmetric unit.
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Cite this article as:
Yu Feng, Song Jiaping, Xu Chunyan, Ding Yu, Hu Xiaojian, He Jianhua and Zhang Zhihong, Crystallization and Preliminary X-Ray Analysis of Sau3AI C-Terminal 232-419 Amino Acids Fragment, Protein & Peptide Letters 2006; 13 (6) . https://dx.doi.org/10.2174/092986606777145724
DOI https://dx.doi.org/10.2174/092986606777145724 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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