2I3F

Crystal Structure of a Glycolipid transfer-like protein from Galdieria sulphuraria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2006-08-04
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97925
Spacegroup name	C 1 2 1
Unit cell lengths	118.438, 48.195, 89.411
Unit cell angles	90.00, 115.06, 90.00

Refinement procedure

Resolution	43.963 - 1.380
R-factor	0.184
Rwork	0.182
R-free	0.21300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	FFAS03 homology model based on PDB 1tfj
RMSD bond length	0.020
RMSD bond angle	1.781
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	43.963	43.963	1.430
High resolution limit [Å]	1.380	2.970	1.380
Rmerge	0.036	0.028	0.246
Number of reflections	93177
<I/σ(I)>	17.474		3.754
Completeness [%]	99.1	98.8	92.4
Redundancy	3.6	3.7	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.0003 M TCEP, 0.005 M Tris PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (16% PEG 1.5K, 0.050 M HEPES pH 7.5) CRYOPROTECTED WITH WELL SOLUTION WITH 20% glycerol, vapor diffusion, hanging drop, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.0003 M TCEP, 0.005 M Tris PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (16% PEG 1.5K, 0.050 M HEPES pH 7.5) CRYOPROTECTED WITH WELL SOLUTION WITH 20% glycerol, vapor diffusion, hanging drop, temperature 293K