1I0E

CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Temperature [K]	291
Detector technology	DIFFRACTOMETER
Detector	WEISSENBERG
Wavelength(s)	1.00
Spacegroup name	P 31 1 2
Unit cell lengths	89.326, 89.326, 402.962
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 3.500
R-factor	0.211
Rwork	0.211
R-free	0.28600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	rabbit muscle creatine kinase
RMSD bond length	0.008
RMSD bond angle	22.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.620
High resolution limit [Å]	3.500	3.500
Rmerge	0.118	0.344
Total number of observations	63933 *
Number of reflections	21262
<I/σ(I)>		2
Completeness [%]	0.9	93.5 *
Redundancy	3	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8 *	291	Tang, L., (1998) Acta Crystallogr., D55, 669. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)	pH5.8
2	1	drop	MPD	40 (%)
3	1	reservoir	MPD	40 (%)