1HZ9

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	1999-05-01
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	I 41
Unit cell lengths	77.445, 77.445, 46.771
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.000 - 1.800
R-factor	0.185 *
Rwork	0.185
R-free	0.23400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c9o
RMSD bond length	0.011
RMSD bond angle	2.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.000	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.035	0.297 *
Number of reflections	12265
<I/σ(I)>	17.9	1.1
Completeness [%]	94.7	68.3 *
Redundancy	3.1 *	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	MPD, Na-Hepes, pH 7.5, 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	MPD	62 (%)
4	1	reservoir	sodium HEPES	100 (mM)