1KP0

The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-18B
Synchrotron site	Photon Factory
Beamline	BL-18B
Temperature [K]	293
Detector technology	CCD
Collection date	2001-02-16
Detector	ADSC QUANTUM 4
Wavelength(s)	1.00
Spacegroup name	I 2 2 2
Unit cell lengths	111.263, 113.624, 191.649
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.700
R-factor	0.191
Rwork	0.188
R-free	0.22200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1chm
RMSD bond length	0.007
RMSD bond angle	1.320 *
Data reduction software	DPS
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.850
High resolution limit [Å]	2.700	2.700
Rmerge	0.065	0.151
Total number of observations	167670 *
Number of reflections	33902
<I/σ(I)>	10.6	4.9
Completeness [%]	99.8	99.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	298	PEG 6000, Na citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.0 (mg/ml)
2	1	reservoir	PEG6000	10 (%)
3	1	reservoir	sodium citrate	0.1 (M)	pH5.0