Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-113 |
Sentence |
denotes |
Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. |
T1 |
0-113 |
Sentence |
denotes |
Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. |
T2 |
114-212 |
Sentence |
denotes |
A protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. |
T2 |
114-212 |
Sentence |
denotes |
A protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. |
T3 |
213-344 |
Sentence |
denotes |
The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. |
T3 |
213-344 |
Sentence |
denotes |
The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. |
T4 |
345-441 |
Sentence |
denotes |
Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. |
T4 |
345-441 |
Sentence |
denotes |
Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. |
T5 |
442-551 |
Sentence |
denotes |
The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. |
T5 |
442-551 |
Sentence |
denotes |
The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. |
T6 |
552-657 |
Sentence |
denotes |
Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. |
T6 |
552-657 |
Sentence |
denotes |
Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. |
T7 |
658-861 |
Sentence |
denotes |
The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. |
T7 |
658-861 |
Sentence |
denotes |
The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. |
T8 |
862-947 |
Sentence |
denotes |
Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. |
T8 |
862-947 |
Sentence |
denotes |
Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. |
T9 |
948-1023 |
Sentence |
denotes |
The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation. |
T9 |
948-1023 |
Sentence |
denotes |
The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation. |