Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration:hydration state 1.

Improving Diffraction by Humidity Control: A Novel Device Compatible with X-Ray Beamlines.

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

MLSVRVAAAVARALPRRAGLVSKNALGSSFIAARNLHASNSRLQKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDG
IARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDG
KGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKK
KLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVA
YRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELF
YKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMA
IEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA

MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLP
PILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKT
KQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERT
REGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSA
LLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDP
LDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGK
LVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS

MFSRAGVAGLSAWTVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKA
DIKTPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTHSDQFLVTFKEVGRRP
PTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSLANIIYY
SLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD

DATA WERE COLLECTED AT ROOM TEMPERATURE DURING CONTROLLED DEHYDRATION OF THE CRYSTALS IN ORDER TO EVALUATE CHANGES IN CRYSTAL PACKING

50 MM TRIS-HCL PH 8.2, 200 MM NACL, 20 MM MGSO4, 1 MM ADP, 1 MM ALCL3, 6 MM NAF 0.004% (W/V)PHENYLMETHYLSULFONYL FLUORIDE AND 12% (W/V) POLYETHYLENE GLYCOL 6000

THE STRUCTURES OF F1-ATPASE INHIBITED BY RESVERATROL, PICEATANNOL AND QUERCETIN.

THE STRUCTURE OF F1-ATPASE INHIBITED BY I1 -60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.

THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN

THE STRUCTURE OF F1-ATPASE INHIBITED BY PICEATANNOL.

BERYLLIUM FLUORIDE INHIBITED BOVINE F1-ATPASE

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B

BOVINE MITOCHONDRIAL F1-ATPASE INHIBITED BY MG2+ADP AND ALUMINIUM FLUORIDE

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN IF1

MOLECULAR ARCHITECTURE OF THE ROTARY MOTOR IN ATP SYNTHASE FROM YEASTMITOCHONDRIA

GROUND STATE STRUCTURE OF F1-ATPASE FROM BOVINE HEART MITOCHONDRIA (BOVINE F1-ATPASE CRYSTALLISED IN THE ABSENCE OF AZIDE)

(ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE ( ALL THREE CATALYTIC SITES OCCUPIED)

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN

THE STRUCTURES OF F1-ATPASE INHIBITED BY QUERCETIN.

BOVINE F1-ATPASE INHIBITED BY DCCD( DICYCLOHEXYLCARBODIIMIDE)

LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 3.

LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 4B.

LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 5.

LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 2.

LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 4A.

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 13-STRANDED BARREL THIS IS REPRESENTED BY
A 14-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS STRUCTURE WAS DETERMINED TO EVALUATE CHANGING CRYSTAL CONTACTS DURING CONTROLLED DEHYDRATION OF CRYSTALS. NO BIOLOGICAL RELEVANCE SHOULD BE GIVEN TO THESE COORDINATES
ATP PHOSPHORYLASE (H+ TRANSPORTING), TRANSIT PEPTIDE, F1FO ATP PHOSPHORYLASE, ION TRANSPORT, ATP SYNTHESIS, UBL CONJUGATION, CF(1), P-LOOP, HYDROLASE, HYDROGEN ION TRANSPORT, PYRROLIDONE CARBOXYLIC ACID