1I5F

BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-05-19
Detector	MARRESEARCH
Wavelength(s)	0.9493
Spacegroup name	I 41
Unit cell lengths	77.120, 77.120, 48.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.400
R-factor	0.139
Rwork	0.139
R-free	0.20500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c9o
RMSD bond length	0.007 *
RMSD bond angle	0.023 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.410
High resolution limit [Å]	1.400	1.400
Rmerge	0.044 *	0.329 *
Number of reflections	26715
<I/σ(I)>	18.9	2.6
Completeness [%]	96.0 *	92.6 *
Redundancy	5.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	PEG 6000, sodium citrate, ammonia sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	sodium-HEPES	10 (mM)
3	1	reservoir	PEG6000	30 (%)
4	1	reservoir	sodium citrate	100 (mM)
5	1	reservoir	ammonium sulfate	200 (mM)