1ZLX

The apo structure of human glycinamide ribonucleotide transformylase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1996-08-16
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 32 2 1
Unit cell lengths	75.660, 75.660, 101.690
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.200 - 2.200
Rwork	0.224
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Truncated (70% remaining) E. coli Glycinamide ribonucleotide transformylase 1GAR
RMSD bond length	0.007
RMSD bond angle	1.340
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]	40.200	2.150
High resolution limit [Å]	2.050	2.050
Number of reflections	16557
<I/σ(I)>	8.3
Completeness [%]	75.8	3
Redundancy	6.9

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
2	VAPOR DIFFUSION, SITTING DROP	6.3	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, 10% 2-propanol (v/v), 18% PEG-4000 (w/v)), pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 300K