1CG2

CARBOXYPEPTIDASE G2

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-04-18
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	81.260, 105.280, 122.190
Unit cell angles	90.00, 109.54, 90.00

Refinement procedure

Resolution	20.000 - 2.500
R-factor	0.196
Rwork	0.196
R-free	0.22400
Structure solution method	MIR
RMSD bond length	0.007
RMSD bond angle	24.310 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.630
High resolution limit [Å]	2.500	2.500
Rmerge	0.069	0.168
Total number of observations	224872 *
Number of reflections	62936
<I/σ(I)>	6.41	4
Completeness [%]	93.9	90.4
Redundancy	3.57	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	291	HANGING DROPS WERE FORMED BY MIXING 4 MICROLITERS OF PROTEIN SOLUTION AT 16-20 MG/ML WITH 4 MICROLITERS OF RESERVOIR SOLUTION CONTAINING 10-12% PEG 4000, 0.2M TRIS (PH 7.2), 0.2M ZINC ACETATE 10% GLYCEROL. CRYSTALS GREW AT 18-20 DEGREES WITHIN A FEW DAYS., vapor diffusion - hanging drop, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	8-10 (mg/ml)
2	1	drop	PEG4000	5-6 (%(w/v))
3	1	drop	zinc acetate	100 (mM)
4	1	drop	Tris-HCl	100 (mM)
5	1	drop	glycerol	5 (%(v/v))
6	1	reservoir	PEG4000	10-12 (%(w/v))
7	1	reservoir	zinc acetate	200 (mM)
8	1	reservoir	Tris-HCl	200 (mM)
9	1	reservoir	glycerol	10 (%(v/v))