Abstract
A photosystem II (PSII) complex highly active in oxygen evolution was purified and crystallized from a thermophilic cyanobacterium, Synechococcus vulcanus. The PSII complex in the crystals contained the D1/D2 reaction center subunits, CP47 and CP43 (two chlorophyll-binding core antenna proteins of photosystem II), cytochrome b-559 α- and β-subunits, several low molecular weight subunits, and three extrinsic proteins, that is, 33 and 12 kDa proteins and cytochrome c-550. The PSII complex also retained a high rate of oxygen evolution. The apparent molecular mass of the PSII in the crystals was determined to be 580 kDa by gel filtration chromatography, indicating that the PSII crystallized is a dimer. The crystals diffracted to a maximum resolution of 3.5 Å at a cryogenic temperature using X-rays from a synchrotron radiation source, SPring-8. The crystals belonged to an orthorhombic system, and the space group was P212121 with unit cell dimensions of a = 129.7 Å b = 226.5 Å and c = 307.8 Å. Each asymmetric unit contained one PSII dimer, which gave rise to a specific volume (V(M)) of 3.6 Å3/Da based on the calculated molecular mass of 310 kDa for a PSII monomer and an estimated solvent content of 66%. Multiple data sets of native crystals have been collected and processed to 4.0 Å, indicating that our crystals are suitable for structure analysis at this resolution.
| Original language | English |
|---|---|
| Pages (from-to) | 14739-14744 |
| Number of pages | 6 |
| Journal | Biochemistry |
| Volume | 39 |
| Issue number | 48 |
| DOIs | |
| Publication status | Published - Dec 5 2000 |
| Externally published | Yes |
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- Biochemistry
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Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus. / Shen, Jian-Ren; Kamiya, N.
In: Biochemistry, Vol. 39, No. 48, 05.12.2000, p. 14739-14744.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus
AU - Shen, Jian-Ren
AU - Kamiya, N.
PY - 2000/12/5
Y1 - 2000/12/5
N2 - A photosystem II (PSII) complex highly active in oxygen evolution was purified and crystallized from a thermophilic cyanobacterium, Synechococcus vulcanus. The PSII complex in the crystals contained the D1/D2 reaction center subunits, CP47 and CP43 (two chlorophyll-binding core antenna proteins of photosystem II), cytochrome b-559 α- and β-subunits, several low molecular weight subunits, and three extrinsic proteins, that is, 33 and 12 kDa proteins and cytochrome c-550. The PSII complex also retained a high rate of oxygen evolution. The apparent molecular mass of the PSII in the crystals was determined to be 580 kDa by gel filtration chromatography, indicating that the PSII crystallized is a dimer. The crystals diffracted to a maximum resolution of 3.5 Å at a cryogenic temperature using X-rays from a synchrotron radiation source, SPring-8. The crystals belonged to an orthorhombic system, and the space group was P212121 with unit cell dimensions of a = 129.7 Å b = 226.5 Å and c = 307.8 Å. Each asymmetric unit contained one PSII dimer, which gave rise to a specific volume (V(M)) of 3.6 Å3/Da based on the calculated molecular mass of 310 kDa for a PSII monomer and an estimated solvent content of 66%. Multiple data sets of native crystals have been collected and processed to 4.0 Å, indicating that our crystals are suitable for structure analysis at this resolution.
AB - A photosystem II (PSII) complex highly active in oxygen evolution was purified and crystallized from a thermophilic cyanobacterium, Synechococcus vulcanus. The PSII complex in the crystals contained the D1/D2 reaction center subunits, CP47 and CP43 (two chlorophyll-binding core antenna proteins of photosystem II), cytochrome b-559 α- and β-subunits, several low molecular weight subunits, and three extrinsic proteins, that is, 33 and 12 kDa proteins and cytochrome c-550. The PSII complex also retained a high rate of oxygen evolution. The apparent molecular mass of the PSII in the crystals was determined to be 580 kDa by gel filtration chromatography, indicating that the PSII crystallized is a dimer. The crystals diffracted to a maximum resolution of 3.5 Å at a cryogenic temperature using X-rays from a synchrotron radiation source, SPring-8. The crystals belonged to an orthorhombic system, and the space group was P212121 with unit cell dimensions of a = 129.7 Å b = 226.5 Å and c = 307.8 Å. Each asymmetric unit contained one PSII dimer, which gave rise to a specific volume (V(M)) of 3.6 Å3/Da based on the calculated molecular mass of 310 kDa for a PSII monomer and an estimated solvent content of 66%. Multiple data sets of native crystals have been collected and processed to 4.0 Å, indicating that our crystals are suitable for structure analysis at this resolution.
UR - http://www.scopus.com/inward/record.url?scp=0034610351&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034610351&partnerID=8YFLogxK
U2 - 10.1021/bi001402m
DO - 10.1021/bi001402m
M3 - Article
C2 - 11101288
AN - SCOPUS:0034610351
VL - 39
SP - 14739
EP - 14744
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 48
ER -