2NYI

Crystal Structure of an Unknown Protein from Galdieria sulphuraria

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-08
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97923, 0.96400
Spacegroup name	P 1 21 1
Unit cell lengths	55.013, 79.991, 55.530
Unit cell angles	90.00, 111.25, 90.00

Refinement procedure

Resolution	45.620 - 1.800
R-factor	0.178
Rwork	0.176
R-free	0.21400
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.287
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	45.620	45.616	1.840
High resolution limit [Å]	1.800	4.440	1.800
Rmerge	0.071	0.051	0.419
Number of reflections	39789
<I/σ(I)>	11.673		2.656
Completeness [%]	96.3	99	83.2
Redundancy	7.4	7.6	4.9

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 MES pH 6.0) mixed in a 1:1 ratio with the well solution (24% PEG 8000, 0.04 M Magnesium chloride, 0.2 M Sodium fluoride, 0.10 M PIPES pH 6.5). Cryoprotection: well solution supplemented with up to 20% ethylene glycol, vapor diffusion, hanging drop, temperature 293K