TY - JOUR
T1 - Expression, purification and crystallization of recombinant human TRAIL
AU - Cha, Sun Shin
AU - Shin, Hang Cheol
AU - Choi, Kwan Yong
AU - Oh, Byung Ha
PY - 1999/5
Y1 - 1999/5
N2 - TRAIL (also known as Apo-2L) belongs to the tumour necrosis factor (TNF) cytokine family and induces rapid apoptosis in a wide variety of tumour cell lines upon binding to the death-signalling receptors on the cell membrane. Normal cells are resistant to TRAIL, owing to the expression of decoy receptors which lack functional death domains and antagonize TRAIL-induced apoptosis. Soluble and functional human TRAIL, expressed in Escherichia coli and refolded into a functional form, has been crystallized. The crystals belong to space group P63 with unit-cell dimensions a = b = 65.61, c = 131.70 Å. The asymmetric unit contains two molecules of TRAIL, with a crystal volume per protein mass (V(m)) of 2.41 Å3 Da-1 and a solvent content of about 42% by volume. A native and a platinum-derivative data set to 2.8 and 3.5 Å resolution, respectively, were obtained from frozen crystals. Structure determination by a combined molecular replacement and isomorphous replacement method is in progress.
AB - TRAIL (also known as Apo-2L) belongs to the tumour necrosis factor (TNF) cytokine family and induces rapid apoptosis in a wide variety of tumour cell lines upon binding to the death-signalling receptors on the cell membrane. Normal cells are resistant to TRAIL, owing to the expression of decoy receptors which lack functional death domains and antagonize TRAIL-induced apoptosis. Soluble and functional human TRAIL, expressed in Escherichia coli and refolded into a functional form, has been crystallized. The crystals belong to space group P63 with unit-cell dimensions a = b = 65.61, c = 131.70 Å. The asymmetric unit contains two molecules of TRAIL, with a crystal volume per protein mass (V(m)) of 2.41 Å3 Da-1 and a solvent content of about 42% by volume. A native and a platinum-derivative data set to 2.8 and 3.5 Å resolution, respectively, were obtained from frozen crystals. Structure determination by a combined molecular replacement and isomorphous replacement method is in progress.
UR - http://www.scopus.com/inward/record.url?scp=0033135957&partnerID=8YFLogxK
U2 - 10.1107/S090744499900164X
DO - 10.1107/S090744499900164X
M3 - Article
C2 - 10216319
AN - SCOPUS:0033135957
SN - 0907-4449
VL - 55
SP - 1101
EP - 1104
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 5
ER -