1OXG

Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	2002-04-14
Detector	MARRESEARCH
Wavelength(s)	0.91
Spacegroup name	I 2 2 2
Unit cell lengths	56.187, 76.382, 105.098
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.690 - 2.200
R-factor	0.198
Rwork	0.192
R-free	0.20700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1acb
RMSD bond length	0.018
RMSD bond angle	2.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.240
High resolution limit [Å]	2.200	2.200
Number of reflections	11673
<I/σ(I)>	18.4	2.9
Completeness [%]	98.7	98.7
Redundancy	20.3	23.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.8	298	0.2M Ammonium sulphate, 20mM Sodium acetate buffer, pH 4.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K