Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Sahil Balotra; Janet Newman; Nigel G. French; Lyndall J. Briggs; Thomas S. Peat; Colin Scott

doi:10.1107/S2053230X13034705

Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Sahil Balotra, Janet Newman, Nigel G. French, Lyndall J. Briggs, Thomas S. Peat, Colin Scott^*

^*Corresponding author for this work

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

8 Citations (Scopus)

24 Downloads (Pure)

Abstract

The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P2₁, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

Original language	English
Pages (from-to)	310-315
Number of pages	6
Journal	Acta Crystallographica. Section F: Structural Biology Communications
Volume	70
Issue number	3
DOIs	https://doi.org/10.1107/S2053230X13034705
Publication status	Published - 2014
Externally published	Yes

Bibliographical note

Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

allphanate hydrolase
amidase domain
AtzF
Pseudomonas sp. strain ADP

Access to Document

10.1107/S2053230X13034705

Publisher version (open access)Final published version, 509 KBLicence: CC BY

Cite this

@article{96b031c3070244f0996ecb1f4f64437c,

title = "Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP",

abstract = "The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 {\AA} resolution and adopted space group P21, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 {\AA}, β = 106.6°.",

keywords = "allphanate hydrolase, amidase domain, AtzF, Pseudomonas sp. strain ADP",

author = "Sahil Balotra and Janet Newman and French, {Nigel G.} and Briggs, {Lyndall J.} and Peat, {Thomas S.} and Colin Scott",

note = "Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.",

year = "2014",

doi = "10.1107/S2053230X13034705",

language = "English",

volume = "70",

pages = "310--315",

journal = "Acta Crystallographica. Section F: Structural Biology Communications",

issn = "2053-230X",

publisher = "Wiley-Blackwell, Wiley",

number = "3",

}

Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP. / Balotra, Sahil; Newman, Janet; French, Nigel G. et al.
In: Acta Crystallographica. Section F: Structural Biology Communications, Vol. 70, No. 3, 2014, p. 310-315.

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

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

AU - Balotra, Sahil

AU - Newman, Janet

AU - French, Nigel G.

AU - Briggs, Lyndall J.

AU - Peat, Thomas S.

AU - Scott, Colin

N1 - Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

PY - 2014

Y1 - 2014

N2 - The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P21, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

AB - The allophanate hydrolase from Pseudomonas sp. strain ADP was expressed and purified, and a tryptic digest fragment was subsequently identified, expressed and purified. This 50 kDa construct retained amidase activity and was crystallized. The crystals diffracted to 2.5 Å resolution and adopted space group P21, with unit-cell parameters a = 82.4, b = 179.2, c = 112.6 Å, β = 106.6°.

KW - allphanate hydrolase

KW - amidase domain

KW - AtzF

KW - Pseudomonas sp. strain ADP

UR - http://www.scopus.com/inward/record.url?scp=84905511021&partnerID=8YFLogxK

U2 - 10.1107/S2053230X13034705

DO - 10.1107/S2053230X13034705

M3 - Article

C2 - 24598916

AN - SCOPUS:84905511021

SN - 2053-230X

VL - 70

SP - 310

EP - 315

JO - Acta Crystallographica. Section F: Structural Biology Communications

JF - Acta Crystallographica. Section F: Structural Biology Communications

IS - 3

ER -

Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this