Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule

Chia Lin Chyan; Po Chung Huang; Ta Hsien Lin; Jian Wen Huang; S. S. Lin; Hsien Bin Huang; Yi Cheng Chen

doi:10.1107/S1744309105023006

Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule

Chia Lin Chyan^*, Po Chung Huang, Ta Hsien Lin, Jian Wen Huang, S. S. Lin, Hsien Bin Huang, Yi Cheng Chen

^*此作品的通信作者

醫學系生物化學科

研究成果: Article › 同行評審

3 引文斯高帕斯（Scopus）

摘要

A hybrid molecule consisting of calmodulin (CaM) and the CaM-binding domain of olfactory nucleotide-gated ion-channel peptide (CaM-OLFp) was purified and crystallized by the hanging-drop vapour-diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X-rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM-OLFp hybrid molecule with a solvent content of 36.42%.

原文	English
頁（從 - 到）	785-787
頁數	3
期刊	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
卷	61
發行號	8
DOIs	https://doi.org/10.1107/S1744309105023006
出版狀態	Published - 8月 2005

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10.1107/S1744309105023006

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title = "Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule",

abstract = "A hybrid molecule consisting of calmodulin (CaM) and the CaM-binding domain of olfactory nucleotide-gated ion-channel peptide (CaM-OLFp) was purified and crystallized by the hanging-drop vapour-diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 {\AA} at cryogenic temperature (100 K) using X-rays from a rotating anode (Cu, wavelength 1.54 {\AA}). The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 64.76, b = 36.23, c = 70.96 {\AA}, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM-OLFp hybrid molecule with a solvent content of 36.42%.",

author = "Chyan, {Chia Lin} and Huang, {Po Chung} and Lin, {Ta Hsien} and Huang, {Jian Wen} and Lin, {S. S.} and Huang, {Hsien Bin} and Chen, {Yi Cheng}",

year = "2005",

month = aug,

doi = "10.1107/S1744309105023006",

language = "English",

volume = "61",

pages = "785--787",

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T1 - Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule

AU - Chyan, Chia Lin

AU - Huang, Po Chung

AU - Lin, Ta Hsien

AU - Huang, Jian Wen

AU - Lin, S. S.

AU - Huang, Hsien Bin

AU - Chen, Yi Cheng

PY - 2005/8

Y1 - 2005/8

N2 - A hybrid molecule consisting of calmodulin (CaM) and the CaM-binding domain of olfactory nucleotide-gated ion-channel peptide (CaM-OLFp) was purified and crystallized by the hanging-drop vapour-diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X-rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM-OLFp hybrid molecule with a solvent content of 36.42%.

AB - A hybrid molecule consisting of calmodulin (CaM) and the CaM-binding domain of olfactory nucleotide-gated ion-channel peptide (CaM-OLFp) was purified and crystallized by the hanging-drop vapour-diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X-rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM-OLFp hybrid molecule with a solvent content of 36.42%.

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JO - Acta Crystallographica Section F:Structural Biology Communications

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SN - 1744-3091

IS - 8

ER -

Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule

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