Crystallization and preliminary X-ray crystallographic analysis of the membrane-binding haemprotein nitrophorin 7 from Rhodnius prolixus.
Nitrophorins (nitric oxide transport proteins) are haemproteins originating from the blood-feeding insect Rhodnius prolixus. They consist of an eight-stranded β-barrel, which classifies them into the lipocalin family. Nitrophorin 7 (NP7) and the E27V mutant protein NP7(E27V) were crystallized at 277 K using the vapour-diffusion method with PEG as the precipitating agent. Data sets for wild-type NP7 and NP7(E27V) were collected to 1.80 Å resolution from single crystals at 100 K using synchrotron radiation. The crystals belonged to space group P2(1), with unit-cell parameters a = 38, b = 67, c = 39 Å, β = 117°. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient (V(M)) of 2.11 Å(3) Da(-1); the solvent content was estimated to be 41.8%.
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany. ogata@mpi-muelheim.mpg.de
Hideaki
H
Ogata
Markus
M
Knipp
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D006420:Hemeproteins / Q000737:chemistry*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012239:Rhodnius / Q000737:chemistry*; D012471:Salivary Proteins and Peptides / Q000737:chemistry*
D006420:Hemeproteins; D012471:Salivary Proteins and Peptides; C090560:nitrophorin