Abstract
mBanana is a novel monomeric red fluorescent protein mutant. It was cloned and expressed in Escherichia coli with 10 histidine residues at its N-terminal. After cleavage of the His tag by TEV protease, the mBanana was further purified and crystallized by the hanging-drop vapor-diffusion technique. The crystals can diffract to 2.0Å resolution and one set of completed data was collected. It showed that the orthorhombic mBanana crystal was in space group P21 with unit cell parameters (48.629, 42.667, 61.714, 90, 111.676, 90) and contained one molecule in one asymmetric unit.
Keywords: mBanana, fluorescent protein, crystallization, preliminary X-ray analysis
Protein & Peptide Letters
Title: Crystallization and Preliminary X-Ray Analysis of Fluorescent Protein mBanana
Volume: 15 Issue: 1
Author(s): Yu Ding, Yangbin Zhou, Yifeng Wu, Jiaping Song, Xiaojian Hu and Zhihong Zhang
Affiliation:
Keywords: mBanana, fluorescent protein, crystallization, preliminary X-ray analysis
Abstract: mBanana is a novel monomeric red fluorescent protein mutant. It was cloned and expressed in Escherichia coli with 10 histidine residues at its N-terminal. After cleavage of the His tag by TEV protease, the mBanana was further purified and crystallized by the hanging-drop vapor-diffusion technique. The crystals can diffract to 2.0Å resolution and one set of completed data was collected. It showed that the orthorhombic mBanana crystal was in space group P21 with unit cell parameters (48.629, 42.667, 61.714, 90, 111.676, 90) and contained one molecule in one asymmetric unit.
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Cite this article as:
Ding Yu, Zhou Yangbin, Wu Yifeng, Song Jiaping, Hu Xiaojian and Zhang Zhihong, Crystallization and Preliminary X-Ray Analysis of Fluorescent Protein mBanana, Protein & Peptide Letters 2008; 15 (1) . https://dx.doi.org/10.2174/092986608783330341
DOI https://dx.doi.org/10.2174/092986608783330341 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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