Please use this identifier to cite or link to this item: https://doi.org/10.1107/S1744309105037681
Title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of Arabidopsis thaliana cyclophilin 38 (AtCyp38)
Authors: Vasudevan, D.
Gopalan, G.
He, Z.
Luan, S.
Swaminathan, K. 
Issue Date: 2005
Citation: Vasudevan, D., Gopalan, G., He, Z., Luan, S., Swaminathan, K. (2005). Expression, purification, crystallization and preliminary X-ray diffraction analysis of Arabidopsis thaliana cyclophilin 38 (AtCyp38). Acta Crystallographica Section F: Structural Biology and Crystallization Communications 61 (12) : 1087-1089. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309105037681
Abstract: AtCyp38 is one of the highly divergent multidomain cyclophilins from Arabidopsis thaliana. A recombinant form of AtCyp38 (residues 83-437) was expressed in Escherichia coli and purified to homogeneity. The protein was crystallized using the vapour-batch technique with PEG 6000 and t-butanol as precipitants. Crystals of recombinant AtCyp38 diffracted X-rays to better than 2.5 Å resolution at 95 K using a synchrotron-radiation source. The crystal belongs to the C-centred orthorhombic space group C2221, with unit-cell parameters a = 58.2, b = 95.9, c = 167.5 Å, and contains one molecule in the asymmetric unit. The selenomethionine derivative of the AtCyp38 protein was overexpressed, purified and crystallized in the same space group and data were collected to 3.5 Å at the NSLS synchrotron. The structure is being solved by the MAD method. © 2005 International Union of Crystallography All rights reserved.
Source Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/100655
ISSN: 17443091
DOI: 10.1107/S1744309105037681
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