1Z3D

Protein crystal growth improvement leading to the 2.5A crystallographic structure of ubiquitin-conjugating enzyme (ubc-1) from Caenorhabditis elegans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Detector	MAR CCD 165 mm
Wavelength(s)	0.97
Spacegroup name	P 65
Unit cell lengths	100.550, 100.550, 35.840
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.030 - 2.500
R-factor	0.242
Rwork	0.242
R-free	0.27300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2aak
RMSD bond length	0.008
RMSD bond angle	1.400
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.590
High resolution limit [Å]	2.500	5.380	2.500
Rmerge	0.058	0.034	0.326
Number of reflections	7370
Completeness [%]	97.1
Redundancy	2.6	2.9	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	COUNTER-DIFFUSION	8.5	277.5	0.1 M Tris, pH 8.5, 0.2 M MgCl2, 30% PEG 4K, counter-diffusion, temperature 277.5K