4LES

2.2 Angstrom Crystal Structure of Conserved Hypothetical Protein from Bacillus anthracis.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-17
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 63
Unit cell lengths	95.754, 95.754, 41.518
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.340 - 2.200
R-factor	0.17693
Rwork	0.175
R-free	0.21151
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.712
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	REFMAC (5.8.0046)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.052	0.522
Number of reflections	11282
<I/σ(I)>	32.2	3.5
Completeness [%]	100.0	100
Redundancy	6.4	6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	295	Protein: 7.4 mG/mL, 0.25 M Sodium chloride, 0.01 M Tris-HCL buffer pH 8.3; Screen: JSCG+ (C6), 0.1 M Phosphate-citrate buffer pH 4.2, 40% (v/v) PEG 300, VAPOR DIFFUSION, SITTING DROP, temperature 295K