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.
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 -