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) |
|---|---|
| Journal | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
| Volume | 51 |
| Issue number | 3-4 |
| State | Published - 1996 |
| Externally published | Yes |
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Keywords
- Crystallization
- Mesophilic Cyanobacterium
- Photosystem I
- PS I Monomers
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
Crystallization of intact and subunit L-deficient monomers from synechocystis PCC 6803 photosystem I. / Jekow, Petra; Schubert, Wolf Dieter; Fromme, Petra; Kruip, Jochen; Chitnis, Parag R.; Rögner, Matthias; Saenger, Wolfram.
In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 51, No. 3-4, 1996.Research output: Contribution to journal › Article
}
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 - Photosystem I
KW - PS I Monomers
UR - http://www.scopus.com/inward/record.url?scp=11344267612&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11344267612&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:11344267612
VL - 51
JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
SN - 0939-5075
IS - 3-4
ER -