1EMA

GREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1		8.2		22-26% PEG 4000, 50 MM HEPES PH 8.0-8.4, 50 MM MGCL2, 10 MM 2-MERCAPTOETHANOL, 5-7 MG PROTEIN, pH 8.2

Crystal Properties
Matthews coefficient	Solvent content
2.1	40.5

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 51.77	�� = 90
b = 62.85	�� = 90
c = 70.67	�� = 90

Symmetry
Space Group	P 21 21 21

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	295	IMAGE PLATE	FUJI		1996-04-28	M

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X4A		NSLS	X4A

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.9		84	0.09		6.45		17676			16.5

Refinement

Statistics
Diffraction ID	Structure Solution Method	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Work	R-Free	Mean Isotropic B
X-RAY DIFFRACTION	MIR/SAD	1.9	20	17676		84

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]

RMS Deviations
Key	Refinement Restraint Deviation
t_dihedral_angle_d	19.65
t_it	4.29
t_angle_deg	1.95
t_nbd	0.041
t_gen_planes	0.018
t_bond_d	0.014
t_trig_c_planes	0.014
t_incorr_chiral_ct
t_pseud_angle

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1771
Nucleic Acid Atoms
Solvent Atoms	95
Heterogen Atoms

Software

Software
Software Name	Purpose
CCP4	model building
PROTEIN	model building
TNT	refinement
HKL	data reduction
HKL	data scaling
CCP4	phasing
PROTEIN	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.