Recrystallization: a method to improve the quality of protein crystals

Hou, Hai; Liu, Yue; Wang, Bo; Jiang, Fan; Tao, Hao-Ran; Hu, Shan-Yang; Yin, Da‐Chuan

doi:10.1107/s1600576715005129

Cited by 4 publications

(5 citation statements)

References 26 publications

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“…Clearly, the diffraction pattern in Figure d shows many diffraction spots, while there was no spot in Figure c, showing that the crystal quality was improved after recrystallization. This result is in good agreement with our previous results …”

Section: Resultssupporting

confidence: 94%

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Direct Crystallization of Proteins from Impure Sources

Liu

Hou

et al. 2020

Crystal Growth & Design

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In recent years, with the rapidly increasing demand for pure protein products in various fields (biomedicines, biochemical reagents, food industries, etc.), the need for low-cost, high-quality protein purification technology has become urgent. Under this background, the traditional purification technology, protein crystallization, comes back to people’s attention. Protein crystallization has the ability to obtain high-quality protein products at a low cost. Nevertheless, protein crystallization itself is challenging; for a long time, the industrial purification of proteins often has used chromatography-based approaches. In the field of structural biology, the strong demand for protein crystals has led to the full development of protein crystallization technology. To date, these technologies may have the potential to provide solutions to achieve crystallization of proteins at the industrial scale. In this paper, we report our effort to screen the crystallization conditions of four sample proteins (lysozyme, hemoglobin, superoxide dismutase, and homoserine oxygen-acetyltransferase) from different impure sources (natural and recombined ones). It was confirmed that crystallization screening technology allows protein crystals to be obtained directly from impure protein sources, showing that, from the impure sources, the target protein can be purified directly by crystallization without prior purification using chromatographic processes. This work demonstrated that the new technologies developed in the field of protein crystallization methodologies can be well applied in solving problems in traditional purification technology.

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Section: Resultssupporting

confidence: 94%

“…This result is in good agreement with our previous results. 57 3.2.2. Hemoglobin Extracted from the Chicken Blood.…”

Section: Resultsmentioning

confidence: 99%

Direct Crystallization of Proteins from Impure Sources

Liu

Hou

et al. 2020

Crystal Growth & Design

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“…Seeds 1: cross-linked lysozyme crystals; seeds 2: cross-linked lysozyme and concanavalin A crystals, with a mass ratio of 1:1, and seeds 3: cross-linked lysozyme, concanavalin A and catalase crystals, with a mass ratio of 1:1:1. According to our routine crystallization screening experiments, the reliable range of crystallization conditions for crystallization experiments [30][31][32] was screened out by us.…”

Section: Methodsmentioning

confidence: 99%

Comparison of the Quality of Protein Crystals Grown by CLPC Seeds Method

Yan

Liu

et al. 2019

Crystals

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We present a systematic quality comparison of protein crystals obtained with and without cross-linked protein crystal (CLPC) seeds. Four proteins were used to conduct the experiments, and the results showed that crystals obtained in the presence of CLPC seeds exhibited a better morphology. In addition, the X-ray diffraction data showed that the CLPC seeds method is a powerful tool to obtain high-quality protein crystals. Therefore, we recommend the use of CLPC seeds in preparing high-quality diffracting protein crystals.

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“…Large-scale production of protein crystals is highly challenging technically. The literatures on protein crystallization are largely about obtaining large single crystals suitable for X-Ray diffraction with the purpose of molecular structure analysis [7][8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%