1ZLY

The structure of human glycinamide ribonucleotide transformylase in complex with alpha,beta-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,dideazafolate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	282
Detector technology	IMAGE PLATE
Collection date	1997-02-25
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 32 2 1
Unit cell lengths	75.900, 75.900, 101.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 - 2.070
R-factor	0.2
Rwork	0.190
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zlx
RMSD bond length	0.006
RMSD bond angle	1.450
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.170
High resolution limit [Å]	2.070	2.070
Number of reflections	19915
<I/σ(I)>	7.7	3.7
Completeness [%]	99.5	3
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	300	5 mg/ml protein in 10 mM Hepes pH 7.5, 1 mM DTE 1:1 with well solution (100 mM Na citrate pH 6.0, 20% 2-propanol (v/v), 20% PEG-4000 (w/v)) , VAPOR DIFFUSION, HANGING DROP, temperature 300K
1	VAPOR DIFFUSION, HANGING DROP	6	300	5 mg/ml protein in 10 mM Hepes pH 7.5, 1 mM DTE 1:1 with well solution (100 mM Na citrate pH 6.0, 20% 2-propanol (v/v), 20% PEG-4000 (w/v)) , VAPOR DIFFUSION, HANGING DROP, temperature 300K