An unfolding/refolding step helps in the crystallization of a poorly soluble protein

Guido Kaulmann; Gottfried J. Palm; Klaus Schilling; Rolf Hilgenfeld; Bernd Wiederanders

doi:10.1107/S0907444903008801

An unfolding/refolding step helps in the crystallization of a poorly soluble protein

Guido Kaulmann, Gottfried J. Palm, Klaus Schilling, Rolf Hilgenfeld, Bernd Wiederanders^*

^*Corresponding author for this work

Institute of Biochemistry

4 Citations (Scopus)

Abstract

A novel strategy is presented that leads to the crystallization of the isolated N-terminal propeptide of human procathepsin S, a proteinase belonging to the cathepsin L-like endopeptidases of the clan CA1 cysteine peptidases.

Original language	English
Journal	Acta Crystallographica - Section D Biological Crystallography
Volume	59
Issue number	7
Pages (from-to)	1243-1245
Number of pages	3
ISSN	0907-4449
DOIs	https://doi.org/10.1107/S0907444903008801
Publication status	Published - 01.07.2003

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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title = "An unfolding/refolding step helps in the crystallization of a poorly soluble protein",

abstract = "A novel strategy is presented that leads to the crystallization of the isolated N-terminal propeptide of human procathepsin S, a proteinase belonging to the cathepsin L-like endopeptidases of the clan CA1 cysteine peptidases.",

author = "Guido Kaulmann and Palm, \{Gottfried J.\} and Klaus Schilling and Rolf Hilgenfeld and Bernd Wiederanders",

year = "2003",

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T1 - An unfolding/refolding step helps in the crystallization of a poorly soluble protein

AU - Kaulmann, Guido

AU - Palm, Gottfried J.

AU - Schilling, Klaus

AU - Hilgenfeld, Rolf

AU - Wiederanders, Bernd

PY - 2003/7/1

Y1 - 2003/7/1

N2 - A novel strategy is presented that leads to the crystallization of the isolated N-terminal propeptide of human procathepsin S, a proteinase belonging to the cathepsin L-like endopeptidases of the clan CA1 cysteine peptidases.

AB - A novel strategy is presented that leads to the crystallization of the isolated N-terminal propeptide of human procathepsin S, a proteinase belonging to the cathepsin L-like endopeptidases of the clan CA1 cysteine peptidases.

UR - https://www.scopus.com/pages/publications/0038116561

U2 - 10.1107/S0907444903008801

DO - 10.1107/S0907444903008801

M3 - Journal articles

C2 - 12832773

AN - SCOPUS:0038116561

SN - 0907-4449

VL - 59

SP - 1243

EP - 1245

JO - Acta Crystallographica - Section D Biological Crystallography

JF - Acta Crystallographica - Section D Biological Crystallography

IS - 7

ER -

An unfolding/refolding step helps in the crystallization of a poorly soluble protein

Abstract

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