1HZC

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 BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-01-31
Detector	MARRESEARCH
Wavelength(s)	0.8428
Spacegroup name	I 41
Unit cell lengths	76.864, 76.864, 48.024
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.320
R-factor	0.139 *
Rwork	0.139
R-free	0.18100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c9o
RMSD bond length	0.015
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]	20.000	1.330
High resolution limit [Å]	1.320	1.320
Rmerge	0.038	0.434
Number of reflections	32636
<I/σ(I)>	37.8	1
Completeness [%]	99.4	97.7
Redundancy	2.7	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	MPD, cacodylate, pH 6.5, 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	54 (%)
4	1	reservoir	cacodylate	100 (mM)