Crystallization of the catalytic domain of murine terminal deoxynucleotidyl transferase.
The catalytic domain of murine terminal deoxynucleotidyl transferase (TdT) has been crystallized in the space group P2(1)2(1)2(1), with unit-cell parameters a = 47.1, b = 86.2, c = 111.7 A. The crystals diffract to a resolution of 2.4 A using synchrotron radiation and a full data set has been collected from the native crystals. The enzyme was shown to be active in the crystalline state.
Sukumar
N
N
Unité de Biochimie Structurale, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France.
Boulé
J B
JB
Expert-Bezançon
N
N
Jourdan
N
N
Lescar
J
J
Rougeon
F
F
Papanicolaou
C
C
Delarue
M
M
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004253:DNA Nucleotidylexotransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D051379:Mice; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D004253:DNA Nucleotidylexotransferase