1JQG

Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2000-01-16
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	48.030, 86.390, 50.550
Unit cell angles	90.00, 100.70, 90.00

Refinement procedure

Resolution	12.000 * - 2.500
R-factor	0.18
Rwork	0.180
R-free	0.23810
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1aye
RMSD bond length	0.011
RMSD bond angle	1.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000 *	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.092	0.344 *
Total number of observations	230224 *
Number of reflections	21449
<I/σ(I)>	15.6	2.5
Completeness [%]	93.2	93

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	8 *	291	used macroseeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	Tris-HCl	5 (mM)	pH8.0
2	1	1		0.001 (mM)
3	1	1	protein	10 (mg/ml)
4	1	2	PEG8000	30 (%(w/v))
5	1	2	sodium acetate	0.2 (M)
6	1	2	sodium cacodylate	0.1 (M)	pH5.5