Cloning, purification, crystallization and preliminary X-ray analysis of the catalytic domain of human receptor-like protein tyrosine phosphatase γ in three different crystal forms

Kish, K.; McDonnell, P.A.; Goldfarb, V.; Gao, M.; Metzler, W.J.; Langley, D.R.; Bryson, J.W.; Kiefer, S.E.; Carpenter, B.; Kostich, W.A.; Westphal, R.S.; Sheriff, S.

doi:10.1107/S1744309111017209

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Amino-acid sequences of the (a) His-Tb-RPTPγ, (b) His-Tb-RPTPγ(825–1128)/(V948I, S970T) and (c) His-Tb-RPTPγ(825–1128)/(C858I, S970T) constructs used to produce protein for crystallization studies. The hexa-His tag and the thrombin cleavage site are underlined; the amino acids from residues 825 to 1128 of RPTPγ are not underlined. The first residue following thrombin cleavage is marked with a down arrow (↓). Residues mutated in the V948I, S970T and C858S, S970T constructs are denoted in red bold letters.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 7| June 2011| Pages 768-774

doi:10.1107/S1744309111017209

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