4QVS

2.1 Angstrom resolution crystal structure of S-layer domain-containing protein (residues 221-444) from Clostridium thermocellum ATCC 27405

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-04
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 2 2 21
Unit cell lengths	65.958, 74.813, 98.398
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.350 - 2.100
R-factor	0.20994
Rwork	0.208
R-free	0.24878
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.814
Data reduction software	xia2
Data scaling software	pointless
Phasing software	PHENIX
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.079	0.620
Number of reflections	14480
<I/σ(I)>	43.56	2.6
Completeness [%]	99.1	95.3
Redundancy	7	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	295	protein: 9.35 mg/mL in 10 mM Tris-HCl pH 8.3, 500 mM NaCl, 5 mM BME, crystallization: The PEGs II Suite G11 (83): 0.5 M Lithium chloride, 0.1 M Tris pH 8.5. 28% (w/v) PEG 6000, cyo: well solution, VAPOR DIFFUSION, SITTING DROP, temperature 295K