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Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin.
Acta Crystallogr D Biol Crystallogr. 2004 Nov; 60(Pt 11):2019-21.AC

Abstract

Regucalcin is a novel calcium ion (Ca(2+)) binding protein that does not contain an EF-hand motif as a Ca(2+)-binding domain and has been demonstrated to play a multi-functional role in many cell types. Human liver regucalcin, consisting of 299 amino-acid residues, was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method in the presence of polyethylene glycol 4000 as a precipitant. A native crystal diffracted to 2.8 A with synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 64.87, b = 52.52, c = 86.38 A, beta = 99.86 degrees . Two molecules most probably exist in the asymmetric unit, corresponding to V(M) = 2.2 A(3) Da(-1). Heavy-atom derivative data were collected and the Pb derivative showed one high-occupancy site per molecule.

Authors+Show Affiliations

Exploratory Research Laboratory, Fujisawa Pharmaceutical Co. Ltd, 5-2-3 Tokodai, Tsukuba, Ibaraki 300-2698, Japan. masaichi_warizaya@po.fujisawa.co.jpNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

15502314

Citation

Warizaya, Masaichi, et al. "Expression, Purification, Crystallization and Preliminary X-ray Diffraction Studies of Human Liver Regucalcin." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 11, 2004, pp. 2019-21.
Warizaya M, Kinoshita T, Yamaoka M, et al. Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2019-21.
Warizaya, M., Kinoshita, T., Yamaoka, M., Shibata, T., Saito, N., Nakajima, H., & Fujii, T. (2004). Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 11), 2019-21.
Warizaya M, et al. Expression, Purification, Crystallization and Preliminary X-ray Diffraction Studies of Human Liver Regucalcin. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2019-21. PubMed PMID: 15502314.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin. AU - Warizaya,Masaichi, AU - Kinoshita,Takayoshi, AU - Yamaoka,Makiko, AU - Shibata,Takashi, AU - Saito,Noriko, AU - Nakajima,Hidenori, AU - Fujii,Takashi, Y1 - 2004/10/20/ PY - 2004/06/11/received PY - 2004/08/19/accepted PY - 2004/10/27/pubmed PY - 2005/5/17/medline PY - 2004/10/27/entrez SP - 2019 EP - 21 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 11 N2 - Regucalcin is a novel calcium ion (Ca(2+)) binding protein that does not contain an EF-hand motif as a Ca(2+)-binding domain and has been demonstrated to play a multi-functional role in many cell types. Human liver regucalcin, consisting of 299 amino-acid residues, was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method in the presence of polyethylene glycol 4000 as a precipitant. A native crystal diffracted to 2.8 A with synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 64.87, b = 52.52, c = 86.38 A, beta = 99.86 degrees . Two molecules most probably exist in the asymmetric unit, corresponding to V(M) = 2.2 A(3) Da(-1). Heavy-atom derivative data were collected and the Pb derivative showed one high-occupancy site per molecule. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15502314/Expression_purification_crystallization_and_preliminary_X_ray_diffraction_studies_of_human_liver_regucalcin_ DB - PRIME DP - Unbound Medicine ER -