5GIV

Crystal structure of M32 carboxypeptidase from Deinococcus radiodurans R1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	RRCAT INDUS-2 BEAMLINE PX-BL21
Synchrotron site	RRCAT INDUS-2
Beamline	PX-BL21
Temperature [K]	100
Detector technology	CCD
Collection date	2014-04-22
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.979470
Spacegroup name	C 2 2 21
Unit cell lengths	134.857, 256.632, 199.214
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.970 - 2.400
R-factor	0.2074
Rwork	0.205
R-free	0.24270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3hoa
RMSD bond length	0.005
RMSD bond angle	0.669
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10_2152: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.970	2.440
High resolution limit [Å]	2.400	2.400
Rmerge	0.151	0.608
Number of reflections	134280
<I/σ(I)>	14.4	2.9
Completeness [%]	99.9	100
Redundancy	6.5	6.5
CC(1/2)	0.995

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH		294	100mM Sodium Cacodylate pH 6.5, 0.2M Mg acetate, 15% Glycerol, 20% Cymal, 20% PEG 8000