Crystallization and Preliminary X-Ray Analysis of Sau3AI C-Terminal 232-419 Amino Acids Fragment

Feng Yu; Jiaping Song; Chunyan Xu; Yu Ding; Xiaojian Hu; Jianhua He; Zhihong Zhang

doi:10.2174/092986606777145724

ISSN: 0929-8665
E-ISSN: 1875-5305

Crystallization and Preliminary X-Ray Analysis of Sau3AI C-Terminal 232-419 Amino Acids Fragment
Authors: Feng Yu¹, Jiaping Song², Chunyan Xu³, Yu Ding⁴, Xiaojian Hu⁵, Jianhua He⁶ and Zhihong Zhang⁷
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¹ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ² Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ³ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ⁴ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ⁵ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ⁶ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China. ⁷ Department of Physiology and Biophysics, Fudan University, Shanghai 200433, China.
Source: Protein and Peptide Letters, Volume 13, Issue 6, Jun 2006, p. 627 - 628
DOI: https://doi.org/10.2174/092986606777145724
- Available online: 01 Jun 2006

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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2006-06-01

2025-05-24

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Article Type: Research Article

Keyword(s): crystallization; preliminary X-ray analysis; Sau3AI endonuclease

Crystallization and Preliminary X-Ray Analysis of Sau3AI C-Terminal 232-419 Amino Acids Fragment

Abstract

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