1W8Y

Crystal structure of the nitrocefin acyl-DD-peptidase from Actinomadura R39.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2004-03-10
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	103.490, 94.360, 107.200
Unit cell angles	90.00, 94.58, 90.00

Refinement procedure

Resolution	19.940 - 2.400
R-factor	0.22
Rwork	0.220
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1w79
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.800	2.530
High resolution limit [Å]	2.400	2.400
Rmerge	0.100	0.540
Number of reflections	69694
<I/σ(I)>	9.5	2.2
Completeness [%]	86.6	80.5
Redundancy	2.9	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1