A quality comparison of protein crystals grown under containerless conditions generated by diamagnetic levitation, silicone oil and agarose gel. (8th October 2013)
- Record Type:
- Journal Article
- Title:
- A quality comparison of protein crystals grown under containerless conditions generated by diamagnetic levitation, silicone oil and agarose gel. (8th October 2013)
- Main Title:
- A quality comparison of protein crystals grown under containerless conditions generated by diamagnetic levitation, silicone oil and agarose gel
- Authors:
- Cao, Hui‐Ling
Sun, Li‐Hua
Li, Jian
Tang, Lin
Lu, Hui‐Meng
Guo, Yun‐Zhu
He, Jin
Liu, Yong‐Ming
Xie, Xu‐Zhuo
Shen, He‐Fang
Zhang, Chen‐Yan
Guo, Wei‐Hong
Huang, Lin‐Jun
Shang, Peng
He, Jian‐Hua
Yin, Da‐Chuan - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>High‐quality crystals are key to obtaining accurate three‐dimensional structures of proteins using X‐ray diffraction techniques. However, obtaining such protein crystals is often a challenge. Several containerless crystallization techniques have been reported to have the ability to improve crystal quality, but it is unknown which is the most favourable way to grow high‐quality protein crystals. In this paper, a quality comparison of protein crystals which were grown under three containerless conditions provided by diamagnetic levitation, silicone oil and agarose gel was conducted. A control experiment on a vessel wall was also simultaneously carried out. Seven different proteins were crystallized under the four conditions, and the crystal quality was assessed in terms of the resolution limit, the mosaicity and the <italic>R</italic><sub>merge</sub>. It was found that the crystals grown under the three containerless conditions demonstrated better morphology than those of the control. X‐ray diffraction data indicated that the quality of the crystals grown under the three containerless conditions was better than that of the control. Of the three containerless crystallization techniques, the diamagnetic levitation technique exhibited the best performance in enhancing crystal quality. This paper is to our knowledge the first report of improvement of crystal quality using a<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>High‐quality crystals are key to obtaining accurate three‐dimensional structures of proteins using X‐ray diffraction techniques. However, obtaining such protein crystals is often a challenge. Several containerless crystallization techniques have been reported to have the ability to improve crystal quality, but it is unknown which is the most favourable way to grow high‐quality protein crystals. In this paper, a quality comparison of protein crystals which were grown under three containerless conditions provided by diamagnetic levitation, silicone oil and agarose gel was conducted. A control experiment on a vessel wall was also simultaneously carried out. Seven different proteins were crystallized under the four conditions, and the crystal quality was assessed in terms of the resolution limit, the mosaicity and the <italic>R</italic><sub>merge</sub>. It was found that the crystals grown under the three containerless conditions demonstrated better morphology than those of the control. X‐ray diffraction data indicated that the quality of the crystals grown under the three containerless conditions was better than that of the control. Of the three containerless crystallization techniques, the diamagnetic levitation technique exhibited the best performance in enhancing crystal quality. This paper is to our knowledge the first report of improvement of crystal quality using a diamagnetic levitation technique. Crystals obtained from agarose gel demonstrated the second best improvement in crystal quality. The study indicated that the diamagnetic levitation technique is indeed a favourable method for growing high‐quality protein crystals, and its utilization is thus potentially useful in practical efforts to obtain well diffracting protein crystals.</p> </abstract> … (more)
- Is Part Of:
- Acta crystallographica. Volume 69:Part 10(2013:Oct.)
- Journal:
- Acta crystallographica
- Issue:
- Volume 69:Part 10(2013:Oct.)
- Issue Display:
- Volume 69, Issue 10, Part 10 (2013)
- Year:
- 2013
- Volume:
- 69
- Issue:
- 10
- Part:
- 10
- Issue Sort Value:
- 2013-0069-0010-0010
- Page Start:
- 1901
- Page End:
- 1910
- Publication Date:
- 2013-10-08
- Subjects:
- Biomolecules -- Structure -- Periodicals
Physical biochemistry -- Periodicals
X-ray crystallography -- Periodicals
Crystallography -- Periodicals
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http://www.blackwell-synergy.com/loi/ayd ↗
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http://www.iucr.ac.uk/journals/acta/actad.html ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1107/S0907444913016296 ↗
- Languages:
- English
- ISSNs:
- 0907-4449
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
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