Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens

Kyeong Kyu Kim; Kwang Yeon Hwang; Kang Duk Choi; Joo Hyun Kang; Ook Joon Yoo; Se Won Suh

doi:10.1002/prot.340150212

Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens

Kyeong Kyu Kim, Kwang Yeon Hwang, Kang Duk Choi, Joo Hyun Kang, Ook Joon Yoo, Se Won Suh

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

8 Scopus citations

Abstract

Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 × 0.7 × 0.6 mm³ within a month. The crystals belong to the trigonal space group P3₁ (or P3₂), with unit cell dimensions of a= 147.12 Å and c= 131.08 Å. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 Å³/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 Å Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 Å Bragg spacing from native crystals. © 1993 Wiley‐Liss, Inc.

Original language	English
Pages (from-to)	213-215
Number of pages	3
Journal	Proteins: Structure, Function and Bioinformatics
Volume	15
Issue number	2
DOIs	https://doi.org/10.1002/prot.340150212
State	Published - Feb 1993
Externally published	Yes

Keywords

bacterial esterase
crystals
X‐ray diffraction

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10.1002/prot.340150212

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@article{ce25fa78cd9141c399b078edd2f6094e,

title = "Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens",

abstract = "Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 × 0.7 × 0.6 mm3 within a month. The crystals belong to the trigonal space group P31 (or P32), with unit cell dimensions of a= 147.12 {\AA} and c= 131.08 {\AA}. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 {\AA}3/Da and solvent fraction of 51.5\% by volume. The crystals diffract to at least 2.2 {\AA} Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 {\AA} Bragg spacing from native crystals. {\textcopyright} 1993 Wiley‐Liss, Inc.",

keywords = "bacterial esterase, crystals, X‐ray diffraction",

author = "Kim, \{Kyeong Kyu\} and Hwang, \{Kwang Yeon\} and Choi, \{Kang Duk\} and Kang, \{Joo Hyun\} and Yoo, \{Ook Joon\} and Suh, \{Se Won\}",

year = "1993",

month = feb,

doi = "10.1002/prot.340150212",

language = "English",

volume = "15",

pages = "213--215",

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

issn = "0887-3585",

publisher = "Wiley-Liss Inc.",

number = "2",

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TY - JOUR

T1 - Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens

AU - Kim, Kyeong Kyu

AU - Hwang, Kwang Yeon

AU - Choi, Kang Duk

AU - Kang, Joo Hyun

AU - Yoo, Ook Joon

AU - Suh, Se Won

PY - 1993/2

Y1 - 1993/2

N2 - Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 × 0.7 × 0.6 mm3 within a month. The crystals belong to the trigonal space group P31 (or P32), with unit cell dimensions of a= 147.12 Å and c= 131.08 Å. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 Å3/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 Å Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 Å Bragg spacing from native crystals. © 1993 Wiley‐Liss, Inc.

AB - Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 × 0.7 × 0.6 mm3 within a month. The crystals belong to the trigonal space group P31 (or P32), with unit cell dimensions of a= 147.12 Å and c= 131.08 Å. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 Å3/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 Å Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 Å Bragg spacing from native crystals. © 1993 Wiley‐Liss, Inc.

KW - bacterial esterase

KW - crystals

KW - X‐ray diffraction

UR - https://www.scopus.com/pages/publications/0027522850

U2 - 10.1002/prot.340150212

DO - 10.1002/prot.340150212

M3 - Article

C2 - 8441756

AN - SCOPUS:0027522850

SN - 0887-3585

VL - 15

SP - 213

EP - 215

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

IS - 2

ER -

Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens

Abstract

Keywords

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