Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

Walter Pangborn; Mary Erman; Naiyin Li; Brian M. Burkhart; Vladimir Z. Pletnev; William L. Duax; Rodrigo Gutierrez; Alessandra Peirano; Jaime Eyzaguirre; Daniel J. Thiel; Debashis Ghosh

doi:10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

Walter Pangborn
, Mary Erman
, Naiyin Li
, Brian M. Burkhart
, Vladimir Z. Pletnev
, William L. Duax
, Rodrigo Gutierrez
, Alessandra Peirano
, Jaime Eyzaguirre
, Daniel J. Thiel
, Debashis Ghosh

Department of Structural Biology

Hauptman-Woodward Medical Research Institute, Inc.
Russian Academy of Sciences
Pontificia Universidad Católica de Chile
Cornell University
Roswell Park Cancer Institute

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P2₁2₁2₁ and cell dimensions are a = 34.9Å, b = 61.0Å, c = 72.5Å.

Original language	English
Pages (from-to)	523-524
Number of pages	2
Journal	Proteins: Structure, Function and Genetics
Volume	24
Issue number	4
DOIs	https://doi.org/10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N
State	Published - 1996

Keywords

crystallization
crystallography
esterase
synchrotron radiation

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10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

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Pangborn, W., Erman, M., Li, N., Burkhart, B. M., Pletnev, V. Z., Duax, W. L., Gutierrez, R., Peirano, A., Eyzaguirre, J., Thiel, D. J., & Ghosh, D. (1996). Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction. Proteins: Structure, Function and Genetics, 24(4), 523-524. https://doi.org/10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

@article{2abcf87fd753457984096f0b1997cf73,

title = "Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction",

abstract = "Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 {\AA} resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9{\AA}, b = 61.0{\AA}, c = 72.5{\AA}.",

keywords = "crystallization, crystallography, esterase, synchrotron radiation",

author = "Walter Pangborn and Mary Erman and Naiyin Li and Burkhart, \{Brian M.\} and Pletnev, \{Vladimir Z.\} and Duax, \{William L.\} and Rodrigo Gutierrez and Alessandra Peirano and Jaime Eyzaguirre and Thiel, \{Daniel J.\} and Debashis Ghosh",

year = "1996",

doi = "10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N",

language = "English",

volume = "24",

pages = "523--524",

journal = "Proteins: Structure, Function and Genetics",

issn = "0887-3585",

publisher = "Wiley-Liss Inc.",

number = "4",

}

Pangborn, W, Erman, M, Li, N, Burkhart, BM, Pletnev, VZ, Duax, WL, Gutierrez, R, Peirano, A, Eyzaguirre, J, Thiel, DJ & Ghosh, D 1996, 'Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction', Proteins: Structure, Function and Genetics, vol. 24, no. 4, pp. 523-524. https://doi.org/10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

TY - JOUR

T1 - Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

AU - Pangborn, Walter

AU - Erman, Mary

AU - Li, Naiyin

AU - Burkhart, Brian M.

AU - Pletnev, Vladimir Z.

AU - Duax, William L.

AU - Gutierrez, Rodrigo

AU - Peirano, Alessandra

AU - Eyzaguirre, Jaime

AU - Thiel, Daniel J.

AU - Ghosh, Debashis

PY - 1996

Y1 - 1996

N2 - Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9Å, b = 61.0Å, c = 72.5Å.

AB - Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9Å, b = 61.0Å, c = 72.5Å.

KW - crystallization

KW - crystallography

KW - esterase

KW - synchrotron radiation

UR - https://www.scopus.com/pages/publications/9244221582

U2 - 10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

DO - 10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N

M3 - Article

C2 - 8860002

AN - SCOPUS:9244221582

SN - 0887-3585

VL - 24

SP - 523

EP - 524

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 4

ER -

Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

Abstract

Keywords

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