2016-10-12 OBS 2014-09-29 RCSB RCSB 2014-10-08 2014-12-10 2016-10-12
The authors have reprocessed the original data. Entry is replaced by EMD-8391.
Cryo-EM structure of CIP-treated calstabin-bound RYR1-EGTA (class 8) Zalk R, Clarke OB, des Georges A, Grassucci RA, Reiken S, Mancia F, Hendrickson WA, Frank J, Marks AR calcium release, excitation-contraction coupling in muscle, closed-state, alpha solenoid scaffold, six-transmembrane ion channel, EF-hands, calstabin, FKBP12, SPRY 3j8e Zalk R, Clarke OB, des Georges A, Grassucci RA, Reiken S, Mancia F, Hendrickson WA, Frank J, Marks AR Structure of a mammalian ryanodine receptor. NATURE 517 44 49 2015 25470061 doi:10.1038/nature13950 emd_6107.map.gz Image stored as Reals 320 320 320 0 0 0 319 319 319 320 320 320 401.6 401.6 401.6 90.0 90.0 90.0 X Y Z -0.05482063 0.08638421 0.00010523 0.00577506 1
::::EMDATABANK.org::::EMD-6107::::
1.255 1.255 1.255 0.02 Reconstruction of class 8 of the CIP-treated RYR1-EGTA dataset with C4 symmetry imposed
emd_6107.jpg
emd_6107_fsc.xml emd_6107_fsc_1.xml 2 rabbit skeletal muscle type 1 RyR (RyR1), EGTA- and CIP-treated, bound to calstabin2 (FKBP12.6) heterooctamer 2.2 sequence protein Ryanodine Receptor 1 RYR1 2.2 2.2
Closed state, EGTA treated, CIP-treated
4 Tetramer Oryctolagus cuniculus rabbit false GO:0006874 GO:0005219 GO:0016021 GO:0006811 GO:0055085 GO:0070588 GO:0005216 GO:0005262 GO:0005509 GO:0005515 P11716 IPR013333 IPR003877 IPR001870 IPR011992 IPR005821 skeletal muscle protein Peptidyl-prolyl cis-trans isomerase FKBP1B Calstabin-2, FKBP-12.6 true Homo sapiens human Escherichia coli Wait 30 seconds, blot 1.5 seconds, then plunge. ETHANE 100 FEI VITROBOT MARK IV 95 Objective lens astigmatism was corrected at 180,000 times magnification. FIELD EMISSION GUN 25 BRIGHT FIELD -1000 -4000 FLOOD BEAM
4.6 second exposure, 23 frames
GATAN K2 (4k x 4k) 2.26 42138 FEI POLARA 300 01-JUL-2014 GATAN HELIUM 300 31000 5243 REAL 2XOA REAL 1C9H particle 8 C-flat CF-1.2/1.3-2C-T, Protochips Inc, NC
10 mM HEPES, pH 7.5, 1% w/v CHAPS, 1 M NaCl, 2 mM TCEP, 5 mM EGTA, 0.25% w/v CHAPS, 0.001% w/v DOPC (Avanti)
7.5 singleParticle 0.5 degree sampling Relion each particle 4.8 FSC 0.143, gold-standard C4 48200
Movie frames were aligned with Dosegpu_driftcorr. Particles were picked with Arachnid Autopicker and classified and refined with Relion.