1M4L

STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	297
Detector technology	IMAGE PLATE
Collection date	1997-09-01
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.085
Spacegroup name	P 1 21 1
Unit cell lengths	51.687, 60.267, 47.453
Unit cell angles	90.00, 97.47, 90.00

Refinement procedure

Resolution	30.000 - 1.250
Rwork	0.104
R-free	0.14510
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENTERY 1YME
RMSD bond length	0.015
RMSD bond angle	0.030
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.270
High resolution limit [Å]	1.250	1.250
Rmerge	0.066	0.127
Number of reflections	64976
<I/σ(I)>	13.5
Completeness [%]	86.3	36.3
Redundancy	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	7.5 *	5 *	Shoham, G., (1988) Proc.Natl.Acad.Sci.USA., 85, 684. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1		1.0 (M)
2	1	1	Tris-HCl	0.03 (M)	pH7.5
3	1	2		0.2 (M)
4	1	1	Tris-HCl	0.03 (M)	pH7.5