Literature DB >> 3838557

Crystallization of chicken egg white cystatin, a low molecular weight protein inhibitor of cysteine proteinases, and preliminary X-ray diffraction data.

W Bode, J Brzin, V Turk.   

Abstract

The shorter-chain form of chicken egg white cystatin has been crystallized in 1.6 M-phosphate buffer at pH 4.0 by vapour diffusion. The crystals are of trigonal space group P3121 (or P3221), have cell constants a = b = 47.9 A, c = 87.5 A, alpha = beta = 90 degrees, gamma = 120 degrees, and contain one molecule of 12,191 molecular weight per asymmetric unit. They diffract well to about 2.0 A resolution and are suitable for X-ray crystal structure analysis.

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Year:  1985        PMID: 3838557     DOI: 10.1016/0022-2836(85)90098-1

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


  2 in total

1.  Local pH-dependent conformational changes leading to proteolytic susceptibility of cystatin C.

Authors:  P J Berti; A C Storer
Journal:  Biochem J       Date:  1994-09-01       Impact factor: 3.857

2.  The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

Authors:  W Bode; R Engh; D Musil; U Thiele; R Huber; A Karshikov; J Brzin; J Kos; V Turk
Journal:  EMBO J       Date:  1988-08       Impact factor: 11.598

  2 in total

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