Literature DB >> 2038053

Crystallization of human thymidylate synthase.

C A Schiffer1, V J Davisson, D V Santi, R M Stroud.   

Abstract

Human thymidylate synthase has been crystallized in the absence of ligands and diffracts beyond 3.0 A. The protein was cloned and expressed in Escherichia coli and then crystallized from ammonium sulfate in the presence of beta-mercaptoethanol at a variety of pH values. The crystals are trigonal in the space-group P3(1)21; the unit cell dimensions are a = b = 96.7 A, c = 84.1 A.

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Year:  1991        PMID: 2038053     DOI: 10.1016/0022-2836(91)90558-n

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  1 in total

1.  Replacement of Val3 in human thymidylate synthase affects its kinetic properties and intracellular stability .

Authors:  Xiao Huang; Lydia M Gibson; Brittnaie J Bell; Leslie L Lovelace; Maria Marjorette O Peña; Franklin G Berger; Sondra H Berger; Lukasz Lebioda
Journal:  Biochemistry       Date:  2010-03-23       Impact factor: 3.162

  1 in total

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