3BVO

Crystal structure of human co-chaperone protein HscB

Experimental procedure

Experimental method	SINGLE WAVELENGTH
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	2007-12-10
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97934
Spacegroup name	P 1 21 1
Unit cell lengths	63.644, 32.581, 114.362
Unit cell angles	90.00, 105.24, 90.00

Refinement procedure

Resolution	47.750 - 3.000
R-factor	0.24
Rwork	0.236
R-free	0.28800
Structure solution method	SAD
RMSD bond length	0.008
RMSD bond angle	1.047
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.750	47.750	3.110
High resolution limit [Å]	3.000	6.460	3.000
Rmerge	0.086	0.058	0.342
Number of reflections	9770
<I/σ(I)>	10.054		3.022
Completeness [%]	96.7	99.6	79.8
Redundancy	6.3	6.7	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	Protein solution (10 mg/mL Se-Met protein, 0.050 M Sodium chloride, 0.0031 M Sodium azide, 0.0003 M TCEP, 0.005 M Bis-Tris pH 7.0) mixed in a 1:1 ratio with the Well solution (16% PEG 3350, 0.050 M Lithium sulfate, 0.10 M PIPES pH 6.5), cryoprotected with 20% PEG 3350, 0.050 M Lithium sulfate, 0.10 M PIPES pH 6.5 in four steps up to 20% Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 293K