1CKO

STRUCTURE OF MRNA CAPPING ENZYME IN COMPLEX WITH THE CAP ANALOG GPPPG

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX7.2
Synchrotron site	SRS
Beamline	PX7.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-06
Detector	MAR scanner 300 mm plate
Spacegroup name	C 2 2 21
Unit cell lengths	78.476, 164.013, 103.502
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 3.100
R-factor	0.233
Rwork	0.233
R-free	0.31400
Structure solution method	MOLECULAR REPLACEMENT. THE ROTATION FUNCTION WAS SOLVED FOR EACH OF THE TWO DOMAINS SEPARATELY. TRANSLATION WAS PERFORMED WITH THE TWO DOMAINS INDEPENDENTLY BUT SIMULTANEOUSLY.
Starting model (for MR)	OPEN FORM OF PDB ENTRY 1CKM
RMSD bond length	0.015
RMSD bond angle	24.985 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	3.100
Rmerge	0.035
Number of reflections	12014
Completeness [%]	96.8
Redundancy	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6.5		HANGING DROP VAPOR DIFFUSION. 15 MG/ML PROTEIN IN 50 MM TRIS-HCL, 1.3 MM CAP ANALOG (GPPPG) 0.4 M NACL, 2 MM EDTA, 4 MM DTT, PH 7.5 WERE MIXED WITH AN EQUAL VOLUME OF AND EQUILIBRATED AGAINST 50 MM POTASSIUM PHOSPHATE, 5-10% PEG 8000, 2MM ZNCL2 PH 6.5., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	15 (mg/ml)
2	1	1	GpppG	1.3 (mM)
3	1	1	Tris	50 (mM)
4	1	1		400 (mM)
5	1	1	EDTA	2 (mM)
6	1	1	DTT	4 (mM)
7	1	2	potassium phosphate	50 (mM)
8	1	2	PEG8000	5-10 (%)
9	1	2		2 (mM)