Literature DB >> 11092933

Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercurythiosalicylate.

S Pakhomova1, J G Luz, M Kobayashi, D Mellman, J Buck, M E Newcomer.   

Abstract

Retinol dehydratase is a sulfotransferase which is presumed to catalyze the dehydration of its substrate via a transient retinyl sulfate intermediate. Crystals (space group P2(1), unit-cell parameters a = 82.05, b = 66.61, c = 84.90 A, beta = 111.29 degrees ) are significantly improved by covalent modification of the protein with ethylmercury.

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Year:  2000        PMID： 11092933     DOI： 10.1107/s0907444900012671

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN： 0907-4449


  2 in total

1.  para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E[middle dot]PAP complex and reformation of E[middle dot]PAPS.

Authors:  Eduard Tyapochkin; Paul F Cook; Guangping Chen
Journal:  J Biol Chem       Date:  2009-08-25       Impact factor: 5.157

2.  Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method.

Authors:  Takayoshi Kinoshita; Riyo Maruki; Masaichi Warizaya; Hidenori Nakajima; Shintaro Nishimura
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-03-24
  2 in total

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