Small‐angle X‐ray scattering and crosslinking study of the proteins L7/L12 from Escherichia coli ribosomes

Small‐angle X‐ray scattering study of the proteins S1, S8, S15, S16, S20 from Escherichia coli ribosomes

“…The results described in the previous section are in agreement with our previous studies [2,4,19,20] on ribosomal proteins, indicating that these proteins generally are highly elongated with axial ratios from 1:3 to 1:lO. The S8,S15, and S16 proteins seem to belong to a class of proteins having a maximum dimension of about 100 A.…”

The RNA binding properties of ‘native’ protein—protein complexes isolated from the Escherichia coli ribosome

“…Direct evidence for the existence of a L7/12-LlO complex was obtained earlier by the isolation and in vitro reconstitution of a complex, consisting of proteins L7/12 and LlO in a 4 : 1 molar ratio [8,31]. The RNA-binding properties of this complex, presented here, establish that this is indeed biologically significant.…”

Crystallization of ribosomal protein L7/L12 from Escherichia coli

“…Since the dimers of L7/L12 in solution have a length of about 180 A [7] our finding that the c-axis has a length of 138 A suggests that the dimers may be oriented essentially along the c-axis. The long length of these dimers is unusual when compared to other proteins crystallized previously.…”

“…The protein was purified as described previously [7] , and fig.1 shows the electrophoretic pattern of the protein on polyacrylamide gels. The purified protein at an approximate concentration of 20 mg/ml …”