1M21

Crystal structure analysis of the peptide amidase PAM in complex with the competitive inhibitor chymostatin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-07-12
Detector	MARRESEARCH
Wavelength(s)	0.934
Spacegroup name	P 1 21 1
Unit cell lengths	74.598, 62.559, 102.382
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	100.000 * - 1.800
R-factor	0.203
Rwork	0.203
R-free	0.21600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1m22
RMSD bond length	0.007 *
RMSD bond angle	1.389 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.290	1.910
High resolution limit [Å]	1.780 *	1.800
Rmerge	0.099	0.273
Number of reflections	89189 *
<I/σ(I)>	6.1	3
Completeness [%]	98.1 *	79.9
Redundancy	3.7	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	Neumann, S., (2002) Acta Crystallogr., Sect.D, 58, 333. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	13 (%)
2	1	reservoir	HEPES	0.1 (M)	pH7.5
3	1	reservoir	glycerine	20 (%)
4	1	reservoir	sodium azide	0.02 (%)
5	1	drop	protein	24 (mg/ml)