Crystal structure of an ABC transporter ATP-binding protein (TM_1403) from Thermotoga maritima MSB8 at 2.35 A resolution

Joint Center for Structural Genomics (JCSG)

2-crystal monochromator, Si111, 1m long Rh coated bent cylindrical mirror for horizontal and vertical focussing

Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (ho rizontal focusing)

ABC-type multidrug transport system,ATPase component,Antibiotic ABC transporter,ATP-binding protein,putative

54.0% polyethylene glycol 200, 0.2M sodium chloride, 0.1M phosphate-citrate pH 4.28

0.2M sodium chloride, 55.0% polyethylene glycol 200, 0.1M phosphate-citrate pH 4.2

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

1. ZERO OCCUPANCY HYDROGENS WERE INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U FACTORS. 4. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 5. NCS RESTRAINTS WERE APPLIED DURING REFINEMENT USING LSSR (-AUTONCS) IN BUSTER. 6. LIGAND MOLECULES ADENOSINE-5'-DIPHOSPHATE (ADP) ARE MODELED IN EACH CHAIN BASED ON ELECTRON DENSITY AND HOMOLOGOUS STRUCTURES.

Dimer according to analytical size exclusion

PF00005 family protein, P-loop containing nucleoside triphosphate hydrolases fold, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, HYDROLASE