Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A

K  Muchova; R J  Lewis; J A  Brannigan; W A  Offen; D P  Brown; I  Barak; P  Youngman; A J  Wilkinson

doi:10.1107/S0907444998012682

Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A

K Muchova, R J Lewis, J A Brannigan, W A Offen, D P Brown, I Barak, P Youngman, A J Wilkinson

Chemistry

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

Abstract

The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2.5 Angstrom spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 Angstrom spacing using synchrotron radiation.

Original language	English
Pages (from-to)	671-676
Number of pages	6
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	55
Issue number	3
DOIs	https://doi.org/10.1107/S0907444998012682
Publication status	Published - 3 Mar 1999

Bibliographical note

Keywords

BACILLUS-SUBTILIS SPORULATION
GENE-EXPRESSION
TRANSCRIPTION
BINDING

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Cite this

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title = "Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A",

abstract = "The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2.5 Angstrom spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 Angstrom spacing using synchrotron radiation.",

keywords = "BACILLUS-SUBTILIS SPORULATION, GENE-EXPRESSION, TRANSCRIPTION, BINDING",

author = "K Muchova and Lewis, {R J} and Brannigan, {J A} and Offen, {W A} and Brown, {D P} and I Barak and P Youngman and Wilkinson, {A J}",

note = "Copyright {\textcopyright} 1999 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?ad0052",

year = "1999",

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doi = "10.1107/S0907444998012682",

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T1 - Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A

AU - Muchova, K

AU - Lewis, R J

AU - Brannigan, J A

AU - Offen, W A

AU - Brown, D P

AU - Barak, I

AU - Youngman, P

AU - Wilkinson, A J

PY - 1999/3/3

Y1 - 1999/3/3

N2 - The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2.5 Angstrom spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 Angstrom spacing using synchrotron radiation.

AB - The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2.5 Angstrom spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 Angstrom spacing using synchrotron radiation.

KW - BACILLUS-SUBTILIS SPORULATION

KW - GENE-EXPRESSION

KW - TRANSCRIPTION

KW - BINDING

U2 - 10.1107/S0907444998012682

DO - 10.1107/S0907444998012682

M3 - Article

VL - 55

SP - 671

EP - 676

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

SN - 0907-4449

IS - 3

ER -