8ER5

Crystal Structure of NlpC/P60 domain from Clostridium innocuum NlpC/P60 domain-containing protein CI_01448.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-11-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 31 2 1
Unit cell lengths	51.954, 51.954, 157.440
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.620 - 1.920
R-factor	0.1584
Rwork	0.156
R-free	0.20300
Structure solution method	SAD
RMSD bond length	0.005
RMSD bond angle	1.311
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.950
High resolution limit [Å]	1.920	1.920
Rmerge	0.137	0.856
Rmeas	0.149	0.928
Rpim	0.058	0.357
Number of reflections	19632	959
<I/σ(I)>	15.2	2.6
Completeness [%]	99.9	99.8
Redundancy	6.5	6.5
CC(1/2)	0.988	0.779

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	292	Protein: 10.0 mg/ml, 0.25M Sodium chloride, 0.01M Tris pH 8.3; Screen: AmSO4 (G4), 1.0M Ammonium sulfate, 0.1M HEPES sodium salt pH 5.6, 2% (w/v) PEG 400; Cryo: 2M Lithium sulfate