light-independent chlorophyll biosynthetic process / ferredoxin:protochlorophyllide reductase (ATP-dependent) / photosynthesis, dark reaction / oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor / oxidoreductase activity, acting on iron-sulfur proteins as donors / 4 iron, 4 sulfur cluster binding / ATP binding / metal ion binding Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 140 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3.31 Å3/Da / Density % sol: 63 % / Description: NONE
Crystal grow
Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.1 Details: PROTEIN CONCENTRATION = 10 MG/ML TEMPERATURE = 17 DEGREES C ATMOSPHERE - ANAEROBIC, REDUCING METHOD - HANGING DROP VOLUMES - 3MICROL PROTEIN - 3MICROL RESERVOIR SOLUTION RESERVOIR - 9.5% PEG ...Details: PROTEIN CONCENTRATION = 10 MG/ML TEMPERATURE = 17 DEGREES C ATMOSPHERE - ANAEROBIC, REDUCING METHOD - HANGING DROP VOLUMES - 3MICROL PROTEIN - 3MICROL RESERVOIR SOLUTION RESERVOIR - 9.5% PEG 6000, 85MM HEPES PH 7.1, CRYOPROTECTANT - 14% MPD, 15% GLYCEROL
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Data collection
Diffraction
ID
Mean temperature (K)
Crystal-ID
1
100
1
2
100
1
Diffraction source
Source
Site
Beamline
ID
Wavelength
Wavelength (Å)
SYNCHROTRON
ESRF
ID29
1
0.91
SYNCHROTRON
SOLEIL
PROXIMA1
2
0.9790, 0.9795
Detector
Type
ID
Detector
Date
ADSC CCD
1
CCD
Dec 10, 2007
ADSC CCD
2
CCD
Radiation
ID
Protocol
Monochromatic (M) / Laue (L)
Scattering type
Wavelength-ID
1
MAD
M
x-ray
1
2
MAD
M
x-ray
1
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.91
1
2
0.979
1
3
0.9795
1
Reflection
Resolution: 2.4→25 Å / Num. obs: 54878 / % possible obs: 99.1 % / Observed criterion σ(I): 1 / Redundancy: 8.3 % / Biso Wilson estimate: 55.8 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 20
Reflection shell
Resolution: 2.4→2.49 Å / Redundancy: 8.6 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 3.5 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.5.0088
refinement
HKL-2000
datareduction
SCALEPACK
datascaling
SHELX
CDE
phasing
Refinement
Method to determine structure: SIRAS Starting model: NONE Resolution: 2.4→103.65 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.927 / SU B: 19.213 / SU ML: 0.193 / Cross valid method: THROUGHOUT / ESU R: 0.267 / ESU R Free: 0.232 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2569
2817
5.1 %
RANDOM
Rwork
0.20127
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obs
0.20408
52744
98.6 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK