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

Life Sciences School

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

7 Citations (Scopus)

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
Publication status	Published - 1996

Keywords

crystallization
crystallography
esterase
synchrotron radiation

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

Access to Document

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

Cite this

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

Pangborn, Walter ; Erman, Mary ; Li, Naiyin ; Burkhart, Brian M. ; Pletnev, Vladimir Z. ; Duax, William L. ; Gutierrez, Rodrigo ; Peirano, Alessandra ; Eyzaguirre, Jaime ; Thiel, Daniel J. ; Ghosh, Debashis. / Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction. In: Proteins: Structure, Function and Genetics. 1996 ; Vol. 24, No. 4. pp. 523-524.

@article{15da526d22eb4663adfb143da5ca3ccc,

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 Bioinformatics",

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

Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction. / Pangborn, Walter; Erman, Mary; Li, Naiyin; Burkhart, Brian M.; Pletnev, Vladimir Z.; Duax, William L.; Gutierrez, Rodrigo; Peirano, Alessandra; Eyzaguirre, Jaime; Thiel, Daniel J.; Ghosh, Debashis.

In: Proteins: Structure, Function and Genetics, Vol. 24, No. 4, 1996, p. 523-524.

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

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 - http://www.scopus.com/inward/record.url?scp=9244221582&partnerID=8YFLogxK

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

VL - 24

SP - 523

EP - 524

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

SN - 0887-3585

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this