Expression, purification, and crystallization of the catalytic domain of protein tyrosine phosphatase SHP-1.
The catalytic domain of SHP-1, a SH2-domain containing protein tyrosine phosphatase, has been crystallized by the vapor diffusion method using polyethylene glycol as the precipitant. The crystals belong to the monoclinic space group P21 with unit cell dimensions a = 42.12 A, b = 87.94 A, c = 43.22 A, alpha = 90.0 degrees, beta = 120.12 degrees, and gamma = 90.0 degrees. There is one catalytic domain of SHP-1 per asymmetric unit. X-ray was diffracted to at least 2.5 A and the crystals are appropriate for high-resolution structure determination.
Liang
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Program in Molecular Medicine, UMASS Medical Center, Worcester, Massachusetts 01605, USA.
Meng
W
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Niu
T
T
Zhao
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Zhou
G W
GW
D001665:Binding Sites; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D047908:Intracellular Signaling Peptides and Proteins; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011092:Polyethylene Glycols; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11; D053824:Protein Tyrosine Phosphatase, Non-Receptor Type 6; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D054593:SH2 Domain-Containing Protein Tyrosine Phosphatases; D013379:Substrate Specificity
D047908:Intracellular Signaling Peptides and Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11; D053824:Protein Tyrosine Phosphatase, Non-Receptor Type 6; D017027:Protein Tyrosine Phosphatases; D054593:SH2 Domain-Containing Protein Tyrosine Phosphatases