Table 1.
Crystallographic data collection and refinement statistics of ZmPEPC-C4 in complex with Gly
APS, Advanced Photon Source; r.m.s., root mean square.
| Data collectiona | |
| X-ray source | 23-ID B, APS |
| Wavelength (Å) | 0.9793 |
| Space group | P212121 |
| Cell dimensions | |
| a, b, c (Å) | 156.95, 167.24, 242.90 |
| α, β, γ (°) | 90, 90, 90 |
| Rmerge (%) | 12.2 (43.7) |
| I/σ (I) | 11.3 (2.8) |
| Completeness (%) | 93.28 (62.19) |
| Unique reflections | 90,116 (5,966) |
| Redundancy | 3.9 (2.4) |
| Refinement | |
| Resolution range (Å) | 57.1–3.3b (3.4–3.3) |
| Rwork/Rfree (%) | 21.0/25.3 |
| No. of atoms | |
| Protein | 29,265 |
| Glycine | 25 |
| Acetate | 52 |
| Average B-factors (Å2) | |
| Protein | 27.50 |
| Glycine | 12.75 |
| Acetate | 22.77 |
| r.m.s. deviations from ideal stereochemistry | |
| Bond lengths (Å) | 0.007 |
| Bond angles (o) | 0.98 |
| Ramachandran plot | |
| Most favored regions (%) | 94.30 |
| Allowed regions (%) | 5.02 |
| Protein Data Bank code | 5VYJ |
a Values in parentheses correspond to the highest resolution shell.
b Diffracted anisotropically to a resolution of 3.7, 3.3, and 2.7 Å along a*, b*, and c*, respectively. Data were anisotropically truncated and scaled with the Diffraction Anisotropy Server (http://services.mbi.ucla.edu/anisoscale) (Please note that the JBC is not responsible for the long-term archiving and maintenance of this site or any other third party-hosted site.).