1KA2

Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	1999-11-15
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0000
Spacegroup name	C 1 2 1
Unit cell lengths	130.515, 67.106, 67.885
Unit cell angles	90.00, 95.88, 90.00

Refinement procedure

Resolution	19.920 - 2.200
R-factor	0.239
Rwork	0.239
R-free	0.28400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1k9x
RMSD bond length	0.009 *
RMSD bond angle	1.630 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.089	0.278
Total number of observations	147392 *
Number of reflections	29834
<I/σ(I)>	11.8
Completeness [%]	94.8	95.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	4 *	PEG 4000, TRIS, magnesium chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	19 (mg/ml)
2	1	drop	Tris	50 (mM)	pH8.0
3	1	drop	glycerol	10 (%)
4	1	reservoir	PEG4000	25-30 (%)
5	1	reservoir	Tris	100 (mM)	pH8.5
6	1	reservoir		20-40 (mM)