Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I

Petra Jekow; Wolf Dieter Schubert; Petra Fromme; Jochen Kruip; Parag R. Chitnis; Matthias Rögner; Wolfram Saenger

doi:10.1515/znc-1996-3-410

Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I

Petra Jekow, Wolf Dieter Schubert, Petra Fromme, Jochen Kruip, Parag R. Chitnis, Matthias Rögner, Wolfram Saenger

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

8 Scopus citations

Abstract

Photosystem I monomers from wildtype cells of Synechocystis PCC 6803 and from a mutant deficient in the psaL gene were crystallized. PsaL encodes for the hydrophobic subunit L, which has been proposed to constitute the trimerization domain in the PS I trimer. The absence of subunit L facilitated crystallization of the PS I monomer. The unit cell dimensions and the space group for the crystals from this preparation could be determined to be a = b = 132 Å, c = 525 Å, α = β = 90°, y = 120°, the space group is P6₁ or P6₅. The results show the potential of using specifically designed deletion mutants of an integral membrane protein for the systematic improvement of crystal structure data.

Original language	English (US)
Pages (from-to)	195-199
Number of pages	5
Journal	Zeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume	51
Issue number	3-4
DOIs	https://doi.org/10.1515/znc-1996-3-410
State	Published - 1996
Externally published	Yes

Keywords

Crystallization
Mesophilic Cyanobacterium
PS I Monomers
Photosystem I

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1515/znc-1996-3-410

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title = "Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I",

abstract = "Photosystem I monomers from wildtype cells of Synechocystis PCC 6803 and from a mutant deficient in the psaL gene were crystallized. PsaL encodes for the hydrophobic subunit L, which has been proposed to constitute the trimerization domain in the PS I trimer. The absence of subunit L facilitated crystallization of the PS I monomer. The unit cell dimensions and the space group for the crystals from this preparation could be determined to be a = b = 132 {\AA}, c = 525 {\AA}, α = β = 90°, y = 120°, the space group is P61 or P65. The results show the potential of using specifically designed deletion mutants of an integral membrane protein for the systematic improvement of crystal structure data.",

keywords = "Crystallization, Mesophilic Cyanobacterium, PS I Monomers, Photosystem I",

author = "Petra Jekow and Schubert, {Wolf Dieter} and Petra Fromme and Jochen Kruip and Chitnis, {Parag R.} and Matthias R{\"o}gner and Wolfram Saenger",

year = "1996",

doi = "10.1515/znc-1996-3-410",

language = "English (US)",

volume = "51",

pages = "195--199",

journal = "Zeitschrift fur Naturforschung. Teil C: Biochemie, Biophysik, Biologie, Virologie",

issn = "0939-5075",

publisher = "Verlag der Zeitschrift fur Naturforschung",

number = "3-4",

}

TY - JOUR

T1 - Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I

AU - Jekow, Petra

AU - Schubert, Wolf Dieter

AU - Fromme, Petra

AU - Kruip, Jochen

AU - Chitnis, Parag R.

AU - Rögner, Matthias

AU - Saenger, Wolfram

PY - 1996

Y1 - 1996

N2 - Photosystem I monomers from wildtype cells of Synechocystis PCC 6803 and from a mutant deficient in the psaL gene were crystallized. PsaL encodes for the hydrophobic subunit L, which has been proposed to constitute the trimerization domain in the PS I trimer. The absence of subunit L facilitated crystallization of the PS I monomer. The unit cell dimensions and the space group for the crystals from this preparation could be determined to be a = b = 132 Å, c = 525 Å, α = β = 90°, y = 120°, the space group is P61 or P65. The results show the potential of using specifically designed deletion mutants of an integral membrane protein for the systematic improvement of crystal structure data.

AB - Photosystem I monomers from wildtype cells of Synechocystis PCC 6803 and from a mutant deficient in the psaL gene were crystallized. PsaL encodes for the hydrophobic subunit L, which has been proposed to constitute the trimerization domain in the PS I trimer. The absence of subunit L facilitated crystallization of the PS I monomer. The unit cell dimensions and the space group for the crystals from this preparation could be determined to be a = b = 132 Å, c = 525 Å, α = β = 90°, y = 120°, the space group is P61 or P65. The results show the potential of using specifically designed deletion mutants of an integral membrane protein for the systematic improvement of crystal structure data.

KW - Crystallization

KW - Mesophilic Cyanobacterium

KW - PS I Monomers

KW - Photosystem I

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U2 - 10.1515/znc-1996-3-410

DO - 10.1515/znc-1996-3-410

M3 - Article

AN - SCOPUS:11344267612

VL - 51

SP - 195

EP - 199

JO - Zeitschrift fur Naturforschung. Teil C: Biochemie, Biophysik, Biologie, Virologie

JF - Zeitschrift fur Naturforschung. Teil C: Biochemie, Biophysik, Biologie, Virologie

SN - 0939-5075

IS - 3-4

ER -

Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I

Abstract

Keywords

ASJC Scopus subject areas

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